sino biological insect derived sars cov 2 rbd  (Sino Biological)


Bioz Verified Symbol Sino Biological is a verified supplier
Bioz Manufacturer Symbol Sino Biological manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93

    Structured Review

    Sino Biological sino biological insect derived sars cov 2 rbd
    Superimposition of the initial structure (red) and final structure (blue) after 500 ns of simulation of the <t>SARS-CoV-2</t> spike protein bound to (A) control α1 helix and (B) designed peptide modification 15.
    Sino Biological Insect Derived Sars Cov 2 Rbd, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sino biological insect derived sars cov 2 rbd/product/Sino Biological
    Average 93 stars, based on 14 article reviews
    Price from $9.99 to $1999.99
    sino biological insect derived sars cov 2 rbd - by Bioz Stars, 2022-11
    93/100 stars

    Images

    1) Product Images from "Targeting SARS-CoV-2 Receptor Binding Domain with Stapled Peptides: An In Silico Study"

    Article Title: Targeting SARS-CoV-2 Receptor Binding Domain with Stapled Peptides: An In Silico Study

    Journal: The Journal of Physical Chemistry. B

    doi: 10.1021/acs.jpcb.1c02398

    Superimposition of the initial structure (red) and final structure (blue) after 500 ns of simulation of the SARS-CoV-2 spike protein bound to (A) control α1 helix and (B) designed peptide modification 15.
    Figure Legend Snippet: Superimposition of the initial structure (red) and final structure (blue) after 500 ns of simulation of the SARS-CoV-2 spike protein bound to (A) control α1 helix and (B) designed peptide modification 15.

    Techniques Used: Modification

    Spike protein (RBD) of SARS-CoV-2 (yellow) and modification 15 (blue) complex from PATCHDOCK prediction. (A) Detailing of the polar interactions between the substituted Glu residue and Lys417. (B) Detailing of the polar interactions determined by acetylated Lys in modification 15. The nonpolar hydrogens were hidden for visualization purpose.
    Figure Legend Snippet: Spike protein (RBD) of SARS-CoV-2 (yellow) and modification 15 (blue) complex from PATCHDOCK prediction. (A) Detailing of the polar interactions between the substituted Glu residue and Lys417. (B) Detailing of the polar interactions determined by acetylated Lys in modification 15. The nonpolar hydrogens were hidden for visualization purpose.

    Techniques Used: Modification

    Most persistent interactions ( > 10% of simulation time) from modification 11 (A) and modification 15 (B) with viral RBD containing the mutation E484K. Interacting residues from RBD of SARS-CoV-2 (left Y -axis) and from modification 15 (right Y -axis).
    Figure Legend Snippet: Most persistent interactions ( > 10% of simulation time) from modification 11 (A) and modification 15 (B) with viral RBD containing the mutation E484K. Interacting residues from RBD of SARS-CoV-2 (left Y -axis) and from modification 15 (right Y -axis).

    Techniques Used: Modification, Mutagenesis

    RMSD fluctuations of the original 22-mer hACE2 α1 helix (A), NYBSP-4 stapled control (B), modification 15 (C), and modification 11 (D) spike protein of SARS-CoV-2 complexes. The 500 ns MD simulations were monitored with the first frame as a reference. RMSD based on carbon α of the protein (black) (left Y -axis) and ligand RMSD (right Y -axis). Lig fit Prot in blue, and Lig fit Lig in red.
    Figure Legend Snippet: RMSD fluctuations of the original 22-mer hACE2 α1 helix (A), NYBSP-4 stapled control (B), modification 15 (C), and modification 11 (D) spike protein of SARS-CoV-2 complexes. The 500 ns MD simulations were monitored with the first frame as a reference. RMSD based on carbon α of the protein (black) (left Y -axis) and ligand RMSD (right Y -axis). Lig fit Prot in blue, and Lig fit Lig in red.

    Techniques Used: Modification

    Detailing of the aspartic acid 30 substitution by glutamic acid in modification 15. Spike protein (RBD) of SARS-CoV-2 (yellow). Modification 15 (blue) and hACE2 control (cyan) overlaid. The nonpolar hydrogens were hidden for visualization purpose.
    Figure Legend Snippet: Detailing of the aspartic acid 30 substitution by glutamic acid in modification 15. Spike protein (RBD) of SARS-CoV-2 (yellow). Modification 15 (blue) and hACE2 control (cyan) overlaid. The nonpolar hydrogens were hidden for visualization purpose.

    Techniques Used: Modification

    Most persistent interactions ( > 10% of simulation time) from modification 11 (A) and modification 15 (B) with SARS-CoV-2 RBD. Interacting residues from RBD of SARS-CoV-2 (left Y -axis) and from the studied stapled peptides (right Y -axis).
    Figure Legend Snippet: Most persistent interactions ( > 10% of simulation time) from modification 11 (A) and modification 15 (B) with SARS-CoV-2 RBD. Interacting residues from RBD of SARS-CoV-2 (left Y -axis) and from the studied stapled peptides (right Y -axis).

    Techniques Used: Modification

    2) Product Images from "Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD"

    Article Title: Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD

    Journal: bioRxiv

    doi: 10.1101/2020.03.19.999318

    SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).
    Figure Legend Snippet: SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).

    Techniques Used: Derivative Assay, Liquid Chromatography with Mass Spectroscopy

    SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.
    Figure Legend Snippet: SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.

    Techniques Used: Binding Assay, Derivative Assay, Concentration Assay

    MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.
    Figure Legend Snippet: MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.

    Techniques Used: Selection, Binding Assay, Synthesized

    Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.
    Figure Legend Snippet: Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.

    Techniques Used: Derivative Assay, Binding Assay, Sequencing, Negative Control

    3) Product Images from "Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD"

    Article Title: Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD

    Journal: bioRxiv

    doi: 10.1101/2020.03.19.999318

    SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).
    Figure Legend Snippet: SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).

    Techniques Used: Derivative Assay, Liquid Chromatography with Mass Spectroscopy

    SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.
    Figure Legend Snippet: SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.

    Techniques Used: Binding Assay, Derivative Assay, Concentration Assay

    MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.
    Figure Legend Snippet: MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.

    Techniques Used: Selection, Binding Assay, Synthesized

    Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.
    Figure Legend Snippet: Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.

    Techniques Used: Derivative Assay, Binding Assay, Sequencing, Negative Control

    4) Product Images from "Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD"

    Article Title: Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD

    Journal: bioRxiv

    doi: 10.1101/2020.03.19.999318

    SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).
    Figure Legend Snippet: SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).

    Techniques Used: Derivative Assay, Liquid Chromatography with Mass Spectroscopy

    SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.
    Figure Legend Snippet: SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.

    Techniques Used: Binding Assay, Derivative Assay, Concentration Assay

    MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.
    Figure Legend Snippet: MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.

    Techniques Used: Selection, Binding Assay, Synthesized

    Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.
    Figure Legend Snippet: Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.

    Techniques Used: Derivative Assay, Binding Assay, Sequencing, Negative Control

    5) Product Images from "Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD"

    Article Title: Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD

    Journal: bioRxiv

    doi: 10.1101/2020.03.19.999318

    SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).
    Figure Legend Snippet: SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).

    Techniques Used: Derivative Assay, Liquid Chromatography with Mass Spectroscopy

    SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.
    Figure Legend Snippet: SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.

    Techniques Used: Binding Assay, Derivative Assay, Concentration Assay

    MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.
    Figure Legend Snippet: MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.

    Techniques Used: Selection, Binding Assay, Synthesized

    Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.
    Figure Legend Snippet: Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.

    Techniques Used: Derivative Assay, Binding Assay, Sequencing, Negative Control

    6) Product Images from "Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD"

    Article Title: Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD

    Journal: bioRxiv

    doi: 10.1101/2020.03.19.999318

    SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).
    Figure Legend Snippet: SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).

    Techniques Used: Derivative Assay, Liquid Chromatography with Mass Spectroscopy

    SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.
    Figure Legend Snippet: SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.

    Techniques Used: Binding Assay, Derivative Assay, Concentration Assay

    MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.
    Figure Legend Snippet: MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.

    Techniques Used: Selection, Binding Assay, Synthesized

    Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.
    Figure Legend Snippet: Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.

    Techniques Used: Derivative Assay, Binding Assay, Sequencing, Negative Control

    7) Product Images from "Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD"

    Article Title: Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD

    Journal: bioRxiv

    doi: 10.1101/2020.03.19.999318

    SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).
    Figure Legend Snippet: SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).

    Techniques Used: Derivative Assay, Liquid Chromatography with Mass Spectroscopy

    SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.
    Figure Legend Snippet: SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.

    Techniques Used: Binding Assay, Derivative Assay, Concentration Assay

    MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.
    Figure Legend Snippet: MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.

    Techniques Used: Selection, Binding Assay, Synthesized

    Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.
    Figure Legend Snippet: Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.

    Techniques Used: Derivative Assay, Binding Assay, Sequencing, Negative Control

    8) Product Images from "Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD"

    Article Title: Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD

    Journal: bioRxiv

    doi: 10.1101/2020.03.19.999318

    SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).
    Figure Legend Snippet: SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).

    Techniques Used: Derivative Assay, Liquid Chromatography with Mass Spectroscopy

    SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.
    Figure Legend Snippet: SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.

    Techniques Used: Binding Assay, Derivative Assay, Concentration Assay

    MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.
    Figure Legend Snippet: MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.

    Techniques Used: Selection, Binding Assay, Synthesized

    Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.
    Figure Legend Snippet: Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.

    Techniques Used: Derivative Assay, Binding Assay, Sequencing, Negative Control

    9) Product Images from "Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD"

    Article Title: Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD

    Journal: bioRxiv

    doi: 10.1101/2020.03.19.999318

    SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).
    Figure Legend Snippet: SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).

    Techniques Used: Derivative Assay, Liquid Chromatography with Mass Spectroscopy

    SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.
    Figure Legend Snippet: SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.

    Techniques Used: Binding Assay, Derivative Assay, Concentration Assay

    MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.
    Figure Legend Snippet: MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.

    Techniques Used: Selection, Binding Assay, Synthesized

    Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.
    Figure Legend Snippet: Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.

    Techniques Used: Derivative Assay, Binding Assay, Sequencing, Negative Control

    10) Product Images from "Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD"

    Article Title: Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD

    Journal: bioRxiv

    doi: 10.1101/2020.03.19.999318

    SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).
    Figure Legend Snippet: SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).

    Techniques Used: Derivative Assay, Liquid Chromatography with Mass Spectroscopy

    SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.
    Figure Legend Snippet: SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.

    Techniques Used: Binding Assay, Derivative Assay, Concentration Assay

    MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.
    Figure Legend Snippet: MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.

    Techniques Used: Selection, Binding Assay, Synthesized

    Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.
    Figure Legend Snippet: Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.

    Techniques Used: Derivative Assay, Binding Assay, Sequencing, Negative Control

    11) Product Images from "Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD"

    Article Title: Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD

    Journal: bioRxiv

    doi: 10.1101/2020.03.19.999318

    SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).
    Figure Legend Snippet: SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).

    Techniques Used: Derivative Assay, Liquid Chromatography with Mass Spectroscopy

    SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.
    Figure Legend Snippet: SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.

    Techniques Used: Binding Assay, Derivative Assay, Concentration Assay

    MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.
    Figure Legend Snippet: MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.

    Techniques Used: Selection, Binding Assay, Synthesized

    Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.
    Figure Legend Snippet: Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.

    Techniques Used: Derivative Assay, Binding Assay, Sequencing, Negative Control

    12) Product Images from "Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD"

    Article Title: Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD

    Journal: bioRxiv

    doi: 10.1101/2020.03.19.999318

    SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).
    Figure Legend Snippet: SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).

    Techniques Used: Derivative Assay, Liquid Chromatography with Mass Spectroscopy

    ACE2-derived peptides were prepared by solid-phase peptide synthesis. Total ion current chromatograms (TIC) and associated mass spectra of purified N terminal biotinylated SBP1 peptide (A), purified N-terminal biotinylated SBP2 peptide (B), crude SBP1 peptide (C), and crude SBP2 peptide (D).
    Figure Legend Snippet: ACE2-derived peptides were prepared by solid-phase peptide synthesis. Total ion current chromatograms (TIC) and associated mass spectra of purified N terminal biotinylated SBP1 peptide (A), purified N-terminal biotinylated SBP2 peptide (B), crude SBP1 peptide (C), and crude SBP2 peptide (D).

    Techniques Used: Derivative Assay, Purification

    SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.
    Figure Legend Snippet: SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.

    Techniques Used: Binding Assay, Derivative Assay, Concentration Assay

    MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.
    Figure Legend Snippet: MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.

    Techniques Used: Selection, Binding Assay, Synthesized

    Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.
    Figure Legend Snippet: Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.

    Techniques Used: Derivative Assay, Binding Assay, Sequencing, Negative Control

    13) Product Images from "Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD"

    Article Title: Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD

    Journal: bioRxiv

    doi: 10.1101/2020.03.19.999318

    SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).
    Figure Legend Snippet: SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).

    Techniques Used: Derivative Assay, Liquid Chromatography with Mass Spectroscopy

    SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.
    Figure Legend Snippet: SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.

    Techniques Used: Binding Assay, Derivative Assay, Concentration Assay

    MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.
    Figure Legend Snippet: MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.

    Techniques Used: Selection, Binding Assay, Synthesized

    Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.
    Figure Legend Snippet: Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.

    Techniques Used: Derivative Assay, Binding Assay, Sequencing, Negative Control

    14) Product Images from "Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD"

    Article Title: Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD

    Journal: bioRxiv

    doi: 10.1101/2020.03.19.999318

    SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).
    Figure Legend Snippet: SARS-CoV-2 spike protein RBD domains derived from different biological sources display differences in mass distribution profiles. Total ion current chromatograms (TIC) obtained by LC-MS analysis of commercial samples of (A) glycosylated Sino Biological HEK-expressed SARS-CoV-2-RBD (solution in phosphate-buffered saline) and (B) glycosylated Sino Biological insect-derived SARS-CoV-2-RBD with associated deconvoluted mass spectra obtained by integration over the protein peak at ~8 min. The broad bands in the TIC chromatograms of (B) are due to additives present in the vendor-formulated solid powder (10% glycerol, 5% trehalose, 5% mannitol and 0.01% tween-80).

    Techniques Used: Derivative Assay, Liquid Chromatography with Mass Spectroscopy

    SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.
    Figure Legend Snippet: SBP1 does not compete with ACE2 binding to Sino Biological insect-derived SARS-CoV-2-RBD. (A) Association responses of biotinylated ACE2 to Sino Biological insect derived SARS-CoV-2-RBD at different concentrations. The kinetic dissociation constant determined under these conditions was K D , ACE2 = 15 nM. (B and D) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with soluble human ACE2 at different concentrations. (B) shows the BLI traces and (D) shows re-plots of the endpoint association response (nm) as a function of ACE2 concentration. (C and E) Association responses of biotinylated ACE2 with Sino Biological insect-derived SARS-CoV-2-RBD (kept constant at 100 nM) after mixing with SBP1 at different concentrations. (C) shows the BLI traces and (E) shows re-plots of the endpoint association response (nm) as a function of SBP1 concentration.

    Techniques Used: Binding Assay, Derivative Assay, Concentration Assay

    MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.
    Figure Legend Snippet: MD-guided target selection for rapid flow synthesis of a SARS-CoV-2-RBD297 binding peptide. Fragments of ACE2-PD domain are docked against SARS-CoV-2 receptor-binding domain (PDB: 6M17). Low RMSD peptides are rapidly synthesized by fully automated flow peptide synthesis, and binding to glycosylated SARS-CoV-2-RBD is determined by BLI.

    Techniques Used: Selection, Binding Assay, Synthesized

    Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.
    Figure Legend Snippet: Human ACE2-PD domain α-helix 1-derived SBP1 binds only Sino Biological insect-derived SARS-CoV-2-RBD. (A) RMSD for SBP1 docked to SARS-CoV-2-RBD during 200 ns MD simulation. (B) Binding interface between SARS-CoV-2-RBD and SBP1 after 200 ns simulation. Individual RMSD (C) and average RMSD (D) values for SBP1 residues over the course of the 200 ns simulation. Arrows indicate residues contributing key hydrogen bonding interactions (determined using UCSF Chimera, Version 1.12). Individual residues with RMSD below 5 Å arbitrarily colored green. (E) Binding affinity of SBP1 and a scrambled SBP1 sequence to various sources of glycosylated SARS-CoV-2-RBD proteins determined by bio-layer interferometry (BLI). (F) BLI association response of SBP1 to negative control human protein menin and (G) BLI association response of 12-mer SBP2 peptide to Sino Biological insect-derived SARS-CoV-2-RBD.

    Techniques Used: Derivative Assay, Binding Assay, Sequencing, Negative Control

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 96
    Sino Biological insect derived sars cov 2 spike protein rbd
    Small molecule inhibitors of <t>SARS-CoV-2</t> 3CLpro identified through a quantitative HTS
    Insect Derived Sars Cov 2 Spike Protein Rbd, supplied by Sino Biological, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/insect derived sars cov 2 spike protein rbd/product/Sino Biological
    Average 96 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    insect derived sars cov 2 spike protein rbd - by Bioz Stars, 2022-11
    96/100 stars
      Buy from Supplier

    99
    Sino Biological sars cov 2 2019 ncov spike rbd his recombinant protein covid 19 spike rbd research
    SERS detection of <t>SARS-CoV-2</t> spike protein and RBD on peptide-modified substrates. (A) SERS spectra of the unmodified substrate and of both peptide-modified substrates before and after addition of 2 μM spike protein. (B) Comparison of SERS signal from the SBP-PEG 4 -modified surface and in the presence of 2 μM RBD and 2 μM full spike, with highlighted regions indicating important spectral similarities associated with the spike/RBD (maroon shading) and SBP-PEG 4 (teal shading). The spectra are offset for clarity.
    Sars Cov 2 2019 Ncov Spike Rbd His Recombinant Protein Covid 19 Spike Rbd Research, supplied by Sino Biological, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sars cov 2 2019 ncov spike rbd his recombinant protein covid 19 spike rbd research/product/Sino Biological
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    sars cov 2 2019 ncov spike rbd his recombinant protein covid 19 spike rbd research - by Bioz Stars, 2022-11
    99/100 stars
      Buy from Supplier

    93
    Sino Biological sino biological insect derived sars cov 2 rbd
    Superimposition of the initial structure (red) and final structure (blue) after 500 ns of simulation of the <t>SARS-CoV-2</t> spike protein bound to (A) control α1 helix and (B) designed peptide modification 15.
    Sino Biological Insect Derived Sars Cov 2 Rbd, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sino biological insect derived sars cov 2 rbd/product/Sino Biological
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    sino biological insect derived sars cov 2 rbd - by Bioz Stars, 2022-11
    93/100 stars
      Buy from Supplier

    Image Search Results


    Small molecule inhibitors of SARS-CoV-2 3CLpro identified through a quantitative HTS

    Journal: Journal of Biomedical Science

    Article Title: Beyond the vaccines: a glance at the small molecule and peptide-based anti-COVID19 arsenal

    doi: 10.1186/s12929-022-00847-6

    Figure Lengend Snippet: Small molecule inhibitors of SARS-CoV-2 3CLpro identified through a quantitative HTS

    Article Snippet: Resultantly, the biotinylated peptide sequence derived from human ACE2 demonstrated substantial selective binding affinity to Sino Biological insect-derived SARS-CoV-2 spike protein RBD [ ].

    Techniques:

    Nirmatrelvir, GC376-based small molecule SARS-CoV-2 3CLpro inhibitors and small molecules identified through deep neural network-based generative and predictive models

    Journal: Journal of Biomedical Science

    Article Title: Beyond the vaccines: a glance at the small molecule and peptide-based anti-COVID19 arsenal

    doi: 10.1186/s12929-022-00847-6

    Figure Lengend Snippet: Nirmatrelvir, GC376-based small molecule SARS-CoV-2 3CLpro inhibitors and small molecules identified through deep neural network-based generative and predictive models

    Article Snippet: Resultantly, the biotinylated peptide sequence derived from human ACE2 demonstrated substantial selective binding affinity to Sino Biological insect-derived SARS-CoV-2 spike protein RBD [ ].

    Techniques:

    Autophagy inhibitors, S-Protein inhibitors and other chemical architectures as anti-COVID19 scaffolds

    Journal: Journal of Biomedical Science

    Article Title: Beyond the vaccines: a glance at the small molecule and peptide-based anti-COVID19 arsenal

    doi: 10.1186/s12929-022-00847-6

    Figure Lengend Snippet: Autophagy inhibitors, S-Protein inhibitors and other chemical architectures as anti-COVID19 scaffolds

    Article Snippet: Resultantly, the biotinylated peptide sequence derived from human ACE2 demonstrated substantial selective binding affinity to Sino Biological insect-derived SARS-CoV-2 spike protein RBD [ ].

    Techniques:

    SERS detection of SARS-CoV-2 spike protein and RBD on peptide-modified substrates. (A) SERS spectra of the unmodified substrate and of both peptide-modified substrates before and after addition of 2 μM spike protein. (B) Comparison of SERS signal from the SBP-PEG 4 -modified surface and in the presence of 2 μM RBD and 2 μM full spike, with highlighted regions indicating important spectral similarities associated with the spike/RBD (maroon shading) and SBP-PEG 4 (teal shading). The spectra are offset for clarity.

    Journal: ACS Sensors

    Article Title: Catching COVID: Engineering Peptide-Modified Surface-Enhanced Raman Spectroscopy Sensors for SARS-CoV-2

    doi: 10.1021/acssensors.1c01344

    Figure Lengend Snippet: SERS detection of SARS-CoV-2 spike protein and RBD on peptide-modified substrates. (A) SERS spectra of the unmodified substrate and of both peptide-modified substrates before and after addition of 2 μM spike protein. (B) Comparison of SERS signal from the SBP-PEG 4 -modified surface and in the presence of 2 μM RBD and 2 μM full spike, with highlighted regions indicating important spectral similarities associated with the spike/RBD (maroon shading) and SBP-PEG 4 (teal shading). The spectra are offset for clarity.

    Article Snippet: Baculovirus insect-derived SARS-CoV-2 Spike RBD-His (Cat#: 40592-V08B), SARS-CoV-2 Spike S1 + S2-His (Cat#: 40589-V08B1), SARS-CoV Spike RBD-His (Cat#: 40150-V08B2), and MERS-CoV Spike RBD-His (Cat#: 40071-V08B1) were purchased from SinoBiological.

    Techniques: Modification

    Specificity of the SBP-PEG 4 SERS sensor for SARS-CoV-2 RBD (blue) versus SARS-CoV-1 RBD (red) and MERS-CoV RBD (orange). The peptide surfaces (teal) prior to treatment with each RBD (5 μM) are shown below each spectrum, respectively. The spectra are offset for clarity.

    Journal: ACS Sensors

    Article Title: Catching COVID: Engineering Peptide-Modified Surface-Enhanced Raman Spectroscopy Sensors for SARS-CoV-2

    doi: 10.1021/acssensors.1c01344

    Figure Lengend Snippet: Specificity of the SBP-PEG 4 SERS sensor for SARS-CoV-2 RBD (blue) versus SARS-CoV-1 RBD (red) and MERS-CoV RBD (orange). The peptide surfaces (teal) prior to treatment with each RBD (5 μM) are shown below each spectrum, respectively. The spectra are offset for clarity.

    Article Snippet: Baculovirus insect-derived SARS-CoV-2 Spike RBD-His (Cat#: 40592-V08B), SARS-CoV-2 Spike S1 + S2-His (Cat#: 40589-V08B1), SARS-CoV Spike RBD-His (Cat#: 40150-V08B2), and MERS-CoV Spike RBD-His (Cat#: 40071-V08B1) were purchased from SinoBiological.

    Techniques:

    Characterization of peptide-modified sensor for detection of SARS-CoV-2. (A) Schematic of peptide-modified SERS substrates (i) before and (ii) after binding the spike protein of SARS-CoV-2. (B) Sequence and chemical structure of ACE2-derived peptide used to modify surfaces and bind the spike protein. (C) Normalized XPS spectra of SERS substrates showing peptide modification and RBD binding. (D) Atomic composition of surfaces used in (c) showing successful modification and RBD binding. (E) (i) CLSM 3D reconstructed side-view images of immunolabeled SERS surfaces modified with SBP-PEG 4 before and after RBD binding (scale bar = 2 μm). (ii) Relative fluorescence from quantification of integrated density before and after RBD binding ( n = 4, area per n = 156 μm 2 ).

    Journal: ACS Sensors

    Article Title: Catching COVID: Engineering Peptide-Modified Surface-Enhanced Raman Spectroscopy Sensors for SARS-CoV-2

    doi: 10.1021/acssensors.1c01344

    Figure Lengend Snippet: Characterization of peptide-modified sensor for detection of SARS-CoV-2. (A) Schematic of peptide-modified SERS substrates (i) before and (ii) after binding the spike protein of SARS-CoV-2. (B) Sequence and chemical structure of ACE2-derived peptide used to modify surfaces and bind the spike protein. (C) Normalized XPS spectra of SERS substrates showing peptide modification and RBD binding. (D) Atomic composition of surfaces used in (c) showing successful modification and RBD binding. (E) (i) CLSM 3D reconstructed side-view images of immunolabeled SERS surfaces modified with SBP-PEG 4 before and after RBD binding (scale bar = 2 μm). (ii) Relative fluorescence from quantification of integrated density before and after RBD binding ( n = 4, area per n = 156 μm 2 ).

    Article Snippet: Baculovirus insect-derived SARS-CoV-2 Spike RBD-His (Cat#: 40592-V08B), SARS-CoV-2 Spike S1 + S2-His (Cat#: 40589-V08B1), SARS-CoV Spike RBD-His (Cat#: 40150-V08B2), and MERS-CoV Spike RBD-His (Cat#: 40071-V08B1) were purchased from SinoBiological.

    Techniques: Modification, Binding Assay, Sequencing, Derivative Assay, Confocal Laser Scanning Microscopy, Immunolabeling, Fluorescence

    Linker affects binding affinity of ACE2-derived peptides for RBD. (A) Steady-state analysis of BLI data to determine K d values. (B) CD spectra of cysteine-modified peptides with and without a linker comparing the ability of each to form α-helical structures. (C) BLI response of SBP-PEG 4 showing specific binding to RBD from SARS-CoV-2 compared to SARS-CoV-1 and MERS.

    Journal: ACS Sensors

    Article Title: Catching COVID: Engineering Peptide-Modified Surface-Enhanced Raman Spectroscopy Sensors for SARS-CoV-2

    doi: 10.1021/acssensors.1c01344

    Figure Lengend Snippet: Linker affects binding affinity of ACE2-derived peptides for RBD. (A) Steady-state analysis of BLI data to determine K d values. (B) CD spectra of cysteine-modified peptides with and without a linker comparing the ability of each to form α-helical structures. (C) BLI response of SBP-PEG 4 showing specific binding to RBD from SARS-CoV-2 compared to SARS-CoV-1 and MERS.

    Article Snippet: Baculovirus insect-derived SARS-CoV-2 Spike RBD-His (Cat#: 40592-V08B), SARS-CoV-2 Spike S1 + S2-His (Cat#: 40589-V08B1), SARS-CoV Spike RBD-His (Cat#: 40150-V08B2), and MERS-CoV Spike RBD-His (Cat#: 40071-V08B1) were purchased from SinoBiological.

    Techniques: Binding Assay, Derivative Assay, Modification

    pGX9501 derived more effective specific cytotoxic lymphocyte(CTL) killing ability in vivo and enhanced cytotoxic cytokine expression of specific CD8+ T cell. Single suspension lymphocytes of spleens or lymph nodes from immunized C57BL/6 (A) and Balb/C (B) mice were stimulated with 10 mg/mL SARS-CoV-2 peptide pools in vitro for 4 to 6 hours. Levels of IFN-γ and TNF-α production in CD8+ T cells were measured by flow cytometry. C, Antigen specific cytotoxic lymphocyte(CTL) killing ability was evaluated by an in vivo CTL assay. Target cells at 4*10 6 /ml from naïve mice labelled with a higher concentration of eFlour450 were incubated with 10 mg/mL SARS-CoV-2 peptide pools in vitro for 4-6h before transferring into the immunized mice intravenously. The intensity of eFlour450 peptide labelled target cells was compared with the non-peptide labelled negative control cells after 5 hrs by flow cytometry.

    Journal: bioRxiv

    Article Title: Comparison of Wild Type DNA Sequence of Spike Protein from SARS-CoV-2 with Optimized Sequence on The Induction of Protective Responses Against SARS-Cov-2 Challenge in Mouse Model

    doi: 10.1101/2021.08.13.456164

    Figure Lengend Snippet: pGX9501 derived more effective specific cytotoxic lymphocyte(CTL) killing ability in vivo and enhanced cytotoxic cytokine expression of specific CD8+ T cell. Single suspension lymphocytes of spleens or lymph nodes from immunized C57BL/6 (A) and Balb/C (B) mice were stimulated with 10 mg/mL SARS-CoV-2 peptide pools in vitro for 4 to 6 hours. Levels of IFN-γ and TNF-α production in CD8+ T cells were measured by flow cytometry. C, Antigen specific cytotoxic lymphocyte(CTL) killing ability was evaluated by an in vivo CTL assay. Target cells at 4*10 6 /ml from naïve mice labelled with a higher concentration of eFlour450 were incubated with 10 mg/mL SARS-CoV-2 peptide pools in vitro for 4-6h before transferring into the immunized mice intravenously. The intensity of eFlour450 peptide labelled target cells was compared with the non-peptide labelled negative control cells after 5 hrs by flow cytometry.

    Article Snippet: Briefly, 96-well plates were respectively coated with 0.5μg/ml of pre-S1 (Sino biological, 40591-V05H1), 0.5μg/ml of pre-S2 (Sino biological, 40590-V08B), and 0.17ug/ml of RBD (Sino biological, 40592-V08B) protein (50 mM carbonate-bicarbonate buffer, pH 9.6) at 4°C overnight and blocked with 5% BSA in PBST (0.05% Tween 20 in PBS) at 37°C for 1 hour.

    Techniques: Derivative Assay, In Vivo, Expressing, Mouse Assay, In Vitro, Flow Cytometry, CTL Assay, Concentration Assay, Incubation, Transferring, Negative Control

    pGX9501 promoted TH1-associated cytokine and did not affect TH2-associated cytokine. Single suspension of splenocytes and lymphoid cells of lymph nodes harvested from C57BL/6 (A) or BALB/c (B) mice immunized were stimulated with 10 mg/mL SARS-CoV-2 peptide pools in vitro for 4 to 6 hours, and IFN-□ production of CD4 + T cells was measured by flow cytometry. Both in C57BL/6 and Balb/C mice model. The specific Th2-cytokine expression was verified with the SARS-CoV-2 peptide pool.

    Journal: bioRxiv

    Article Title: Comparison of Wild Type DNA Sequence of Spike Protein from SARS-CoV-2 with Optimized Sequence on The Induction of Protective Responses Against SARS-Cov-2 Challenge in Mouse Model

    doi: 10.1101/2021.08.13.456164

    Figure Lengend Snippet: pGX9501 promoted TH1-associated cytokine and did not affect TH2-associated cytokine. Single suspension of splenocytes and lymphoid cells of lymph nodes harvested from C57BL/6 (A) or BALB/c (B) mice immunized were stimulated with 10 mg/mL SARS-CoV-2 peptide pools in vitro for 4 to 6 hours, and IFN-□ production of CD4 + T cells was measured by flow cytometry. Both in C57BL/6 and Balb/C mice model. The specific Th2-cytokine expression was verified with the SARS-CoV-2 peptide pool.

    Article Snippet: Briefly, 96-well plates were respectively coated with 0.5μg/ml of pre-S1 (Sino biological, 40591-V05H1), 0.5μg/ml of pre-S2 (Sino biological, 40590-V08B), and 0.17ug/ml of RBD (Sino biological, 40592-V08B) protein (50 mM carbonate-bicarbonate buffer, pH 9.6) at 4°C overnight and blocked with 5% BSA in PBST (0.05% Tween 20 in PBS) at 37°C for 1 hour.

    Techniques: Mouse Assay, In Vitro, Flow Cytometry, Expressing

    pGX9501 protects against disease challenges with SARS-CoV-2. Mice treated with the vaccine was challenged by SARS-CoV-2 (10 5 TCID 50 ) in a volume of 100μl 7days after the second immunization (single dose group was challenged by virus 14 days after immunization). Five days after the challenge, Serum was collected for anti-s1 ELISA(A) and Lung was harvested for measuring virus load by qRT-PCR(B). C, Mice treated with the vaccine was challenged by SARS-CoV-2 (10 5 TCID 50 ) in a volume of 100μl 7days after the second immunization (single dose group was challenged by virus 14 days after immunization). Serum was collected for ELISA to evaluate the Neutralizing antibody. D, The histochemistry analysis of lung after H E staining.

    Journal: bioRxiv

    Article Title: Comparison of Wild Type DNA Sequence of Spike Protein from SARS-CoV-2 with Optimized Sequence on The Induction of Protective Responses Against SARS-Cov-2 Challenge in Mouse Model

    doi: 10.1101/2021.08.13.456164

    Figure Lengend Snippet: pGX9501 protects against disease challenges with SARS-CoV-2. Mice treated with the vaccine was challenged by SARS-CoV-2 (10 5 TCID 50 ) in a volume of 100μl 7days after the second immunization (single dose group was challenged by virus 14 days after immunization). Five days after the challenge, Serum was collected for anti-s1 ELISA(A) and Lung was harvested for measuring virus load by qRT-PCR(B). C, Mice treated with the vaccine was challenged by SARS-CoV-2 (10 5 TCID 50 ) in a volume of 100μl 7days after the second immunization (single dose group was challenged by virus 14 days after immunization). Serum was collected for ELISA to evaluate the Neutralizing antibody. D, The histochemistry analysis of lung after H E staining.

    Article Snippet: Briefly, 96-well plates were respectively coated with 0.5μg/ml of pre-S1 (Sino biological, 40591-V05H1), 0.5μg/ml of pre-S2 (Sino biological, 40590-V08B), and 0.17ug/ml of RBD (Sino biological, 40592-V08B) protein (50 mM carbonate-bicarbonate buffer, pH 9.6) at 4°C overnight and blocked with 5% BSA in PBST (0.05% Tween 20 in PBS) at 37°C for 1 hour.

    Techniques: Mouse Assay, Enzyme-linked Immunosorbent Assay, Polymerase Chain Reaction, Staining

    Effects of Antibody Production and Functional Assay. A, The scheme of mice immunizations. B, C57BL/6, or Balb/c mice (n > 5 per group) were either immunized with pVAX1 (blue circle) or vaccinated with pVAX1-S-WT (red square) and pGX9501 (green triangle) intramuscularly, following by electroporation. Serum IgG binding titers (mean ± SEM) to SARS-CoV-2 pre-S1, S2, and RBD were measured on day 28. C, Blocking abilities of RBD binding to the hACE2 with serum samples at serial dilutions on day 28. Data shown represent mean blocking efficiency (mean± SEM) for the five mice.

    Journal: bioRxiv

    Article Title: Comparison of Wild Type DNA Sequence of Spike Protein from SARS-CoV-2 with Optimized Sequence on The Induction of Protective Responses Against SARS-Cov-2 Challenge in Mouse Model

    doi: 10.1101/2021.08.13.456164

    Figure Lengend Snippet: Effects of Antibody Production and Functional Assay. A, The scheme of mice immunizations. B, C57BL/6, or Balb/c mice (n > 5 per group) were either immunized with pVAX1 (blue circle) or vaccinated with pVAX1-S-WT (red square) and pGX9501 (green triangle) intramuscularly, following by electroporation. Serum IgG binding titers (mean ± SEM) to SARS-CoV-2 pre-S1, S2, and RBD were measured on day 28. C, Blocking abilities of RBD binding to the hACE2 with serum samples at serial dilutions on day 28. Data shown represent mean blocking efficiency (mean± SEM) for the five mice.

    Article Snippet: Briefly, 96-well plates were respectively coated with 0.5μg/ml of pre-S1 (Sino biological, 40591-V05H1), 0.5μg/ml of pre-S2 (Sino biological, 40590-V08B), and 0.17ug/ml of RBD (Sino biological, 40592-V08B) protein (50 mM carbonate-bicarbonate buffer, pH 9.6) at 4°C overnight and blocked with 5% BSA in PBST (0.05% Tween 20 in PBS) at 37°C for 1 hour.

    Techniques: Functional Assay, Mouse Assay, Electroporation, Binding Assay, Blocking Assay

    Superimposition of the initial structure (red) and final structure (blue) after 500 ns of simulation of the SARS-CoV-2 spike protein bound to (A) control α1 helix and (B) designed peptide modification 15.

    Journal: The Journal of Physical Chemistry. B

    Article Title: Targeting SARS-CoV-2 Receptor Binding Domain with Stapled Peptides: An In Silico Study

    doi: 10.1021/acs.jpcb.1c02398

    Figure Lengend Snippet: Superimposition of the initial structure (red) and final structure (blue) after 500 ns of simulation of the SARS-CoV-2 spike protein bound to (A) control α1 helix and (B) designed peptide modification 15.

    Article Snippet: Bio-layer interferometry on the top designed peptide showed that the structure presented a dissociation constant, K D , of 1.3 μM for the Sino Biological insect-derived SARS-CoV-2-RBD (the binding of the 23-mer sequence derived from the hACE2 was not reported), a value around 100 times higher compared to the results published by Wrapp et al. for the binding of the hACE2 full length and the spike protein, which determined a K D of ∼14.7 nM.

    Techniques: Modification

    Spike protein (RBD) of SARS-CoV-2 (yellow) and modification 15 (blue) complex from PATCHDOCK prediction. (A) Detailing of the polar interactions between the substituted Glu residue and Lys417. (B) Detailing of the polar interactions determined by acetylated Lys in modification 15. The nonpolar hydrogens were hidden for visualization purpose.

    Journal: The Journal of Physical Chemistry. B

    Article Title: Targeting SARS-CoV-2 Receptor Binding Domain with Stapled Peptides: An In Silico Study

    doi: 10.1021/acs.jpcb.1c02398

    Figure Lengend Snippet: Spike protein (RBD) of SARS-CoV-2 (yellow) and modification 15 (blue) complex from PATCHDOCK prediction. (A) Detailing of the polar interactions between the substituted Glu residue and Lys417. (B) Detailing of the polar interactions determined by acetylated Lys in modification 15. The nonpolar hydrogens were hidden for visualization purpose.

    Article Snippet: Bio-layer interferometry on the top designed peptide showed that the structure presented a dissociation constant, K D , of 1.3 μM for the Sino Biological insect-derived SARS-CoV-2-RBD (the binding of the 23-mer sequence derived from the hACE2 was not reported), a value around 100 times higher compared to the results published by Wrapp et al. for the binding of the hACE2 full length and the spike protein, which determined a K D of ∼14.7 nM.

    Techniques: Modification

    Most persistent interactions ( > 10% of simulation time) from modification 11 (A) and modification 15 (B) with viral RBD containing the mutation E484K. Interacting residues from RBD of SARS-CoV-2 (left Y -axis) and from modification 15 (right Y -axis).

    Journal: The Journal of Physical Chemistry. B

    Article Title: Targeting SARS-CoV-2 Receptor Binding Domain with Stapled Peptides: An In Silico Study

    doi: 10.1021/acs.jpcb.1c02398

    Figure Lengend Snippet: Most persistent interactions ( > 10% of simulation time) from modification 11 (A) and modification 15 (B) with viral RBD containing the mutation E484K. Interacting residues from RBD of SARS-CoV-2 (left Y -axis) and from modification 15 (right Y -axis).

    Article Snippet: Bio-layer interferometry on the top designed peptide showed that the structure presented a dissociation constant, K D , of 1.3 μM for the Sino Biological insect-derived SARS-CoV-2-RBD (the binding of the 23-mer sequence derived from the hACE2 was not reported), a value around 100 times higher compared to the results published by Wrapp et al. for the binding of the hACE2 full length and the spike protein, which determined a K D of ∼14.7 nM.

    Techniques: Modification, Mutagenesis

    RMSD fluctuations of the original 22-mer hACE2 α1 helix (A), NYBSP-4 stapled control (B), modification 15 (C), and modification 11 (D) spike protein of SARS-CoV-2 complexes. The 500 ns MD simulations were monitored with the first frame as a reference. RMSD based on carbon α of the protein (black) (left Y -axis) and ligand RMSD (right Y -axis). Lig fit Prot in blue, and Lig fit Lig in red.

    Journal: The Journal of Physical Chemistry. B

    Article Title: Targeting SARS-CoV-2 Receptor Binding Domain with Stapled Peptides: An In Silico Study

    doi: 10.1021/acs.jpcb.1c02398

    Figure Lengend Snippet: RMSD fluctuations of the original 22-mer hACE2 α1 helix (A), NYBSP-4 stapled control (B), modification 15 (C), and modification 11 (D) spike protein of SARS-CoV-2 complexes. The 500 ns MD simulations were monitored with the first frame as a reference. RMSD based on carbon α of the protein (black) (left Y -axis) and ligand RMSD (right Y -axis). Lig fit Prot in blue, and Lig fit Lig in red.

    Article Snippet: Bio-layer interferometry on the top designed peptide showed that the structure presented a dissociation constant, K D , of 1.3 μM for the Sino Biological insect-derived SARS-CoV-2-RBD (the binding of the 23-mer sequence derived from the hACE2 was not reported), a value around 100 times higher compared to the results published by Wrapp et al. for the binding of the hACE2 full length and the spike protein, which determined a K D of ∼14.7 nM.

    Techniques: Modification

    Detailing of the aspartic acid 30 substitution by glutamic acid in modification 15. Spike protein (RBD) of SARS-CoV-2 (yellow). Modification 15 (blue) and hACE2 control (cyan) overlaid. The nonpolar hydrogens were hidden for visualization purpose.

    Journal: The Journal of Physical Chemistry. B

    Article Title: Targeting SARS-CoV-2 Receptor Binding Domain with Stapled Peptides: An In Silico Study

    doi: 10.1021/acs.jpcb.1c02398

    Figure Lengend Snippet: Detailing of the aspartic acid 30 substitution by glutamic acid in modification 15. Spike protein (RBD) of SARS-CoV-2 (yellow). Modification 15 (blue) and hACE2 control (cyan) overlaid. The nonpolar hydrogens were hidden for visualization purpose.

    Article Snippet: Bio-layer interferometry on the top designed peptide showed that the structure presented a dissociation constant, K D , of 1.3 μM for the Sino Biological insect-derived SARS-CoV-2-RBD (the binding of the 23-mer sequence derived from the hACE2 was not reported), a value around 100 times higher compared to the results published by Wrapp et al. for the binding of the hACE2 full length and the spike protein, which determined a K D of ∼14.7 nM.

    Techniques: Modification

    Most persistent interactions ( > 10% of simulation time) from modification 11 (A) and modification 15 (B) with SARS-CoV-2 RBD. Interacting residues from RBD of SARS-CoV-2 (left Y -axis) and from the studied stapled peptides (right Y -axis).

    Journal: The Journal of Physical Chemistry. B

    Article Title: Targeting SARS-CoV-2 Receptor Binding Domain with Stapled Peptides: An In Silico Study

    doi: 10.1021/acs.jpcb.1c02398

    Figure Lengend Snippet: Most persistent interactions ( > 10% of simulation time) from modification 11 (A) and modification 15 (B) with SARS-CoV-2 RBD. Interacting residues from RBD of SARS-CoV-2 (left Y -axis) and from the studied stapled peptides (right Y -axis).

    Article Snippet: Bio-layer interferometry on the top designed peptide showed that the structure presented a dissociation constant, K D , of 1.3 μM for the Sino Biological insect-derived SARS-CoV-2-RBD (the binding of the 23-mer sequence derived from the hACE2 was not reported), a value around 100 times higher compared to the results published by Wrapp et al. for the binding of the hACE2 full length and the spike protein, which determined a K D of ∼14.7 nM.

    Techniques: Modification