Journal: Biosensors

Article Title: Asymmetric Mach–Zehnder Interferometric Biosensing for Quantitative and Sensitive Multiplex Detection of Anti-SARS-CoV-2 Antibodies in Human Plasma

doi: 10.3390/bios12080553

Figure Lengend Snippet: ( A ) Schematic representation of the binding complex that is formed during the assay. SARS-CoV-2 antigens (NP, RBD, and SP) are immobilized onto the sensor surface; during injection of plasma sample, SARS-CoV-2 specific antibodies (if present) bind to the antigens and, in turn, can be recognized and bound by secondary antibodies during the second incubation step. ( B ) Overlay of sensorgrams obtained for plasma calibrant (1000 IU/mL) and anti-SARS-CoV-2 antibody negative plasma.

Article Snippet: Also shown are sensorgrams ( B) obtained with the Surfix method on a negative control sample (10 times diluted negative plasma in buffer) and a calibrant sample (10 times diluted calibrant stock in buffer).

Techniques: Binding Assay, Injection, Clinical Proteomics, Incubation

Journal: Biosensors

Article Title: Asymmetric Mach–Zehnder Interferometric Biosensing for Quantitative and Sensitive Multiplex Detection of Anti-SARS-CoV-2 Antibodies in Human Plasma

doi: 10.3390/bios12080553

Figure Lengend Snippet: Sensorgrams showing the plasma incubation (direct assay) and the secondary antibody incubation (indirect assay) for ( A ) plasma #27, an anti-SARS-CoV-2 antibody negative plasma (the inset shows a zoom-in), and ( B ) plasma #1, and ( C ) plasma #10, both anti-SARS-CoV-2 antibody positive plasmas.

Article Snippet: Also shown are sensorgrams ( B) obtained with the Surfix method on a negative control sample (10 times diluted negative plasma in buffer) and a calibrant sample (10 times diluted calibrant stock in buffer).

Techniques: Clinical Proteomics, Incubation

Journal: mAbs

Article Title: Preclinical pharmacology, pharmacokinetics, and pharmacodynamics of veligrotug, a full antagonist antibody to the IGF-1 receptor in development for thyroid eye disease

doi: 10.1080/19420862.2025.2585616

Figure Lengend Snippet: Biolayer interferometry screening data for point mutations. (A) Representative biolayer interferometry sensorgrams show the binding of veligrotug and teprotumumab to wild-type human IGF-1R protein, as well as I285A or L286A point mutations. I285A and L286A had minimal effects on binding of veligrotug to IGF-1R. (B) In contrast, I285A reduced binding of teprotumumab to IGF-1R, while L286A completely abrogated binding of teprotumumab to IGF-1R. These results demonstrate that veligrotug and teprotumumab have distinct epitopes.

Article Snippet: The surface plasmon resonance (SPR) sensorgrams from three independent experiments (blue lines) of the response (resonance units) versus time (seconds) of the single cycle kinetics were performed by injecting five increasing concentrations (6.3, 12.5, 25, 50, and 100 nM) of human His-tagged IGF-1R extracellular domain protein over the veligrotug captured on the Biacore chip surface.

Techniques: Binding Assay

Journal: mAbs

Article Title: Preclinical pharmacology, pharmacokinetics, and pharmacodynamics of veligrotug, a full antagonist antibody to the IGF-1 receptor in development for thyroid eye disease

doi: 10.1080/19420862.2025.2585616

Figure Lengend Snippet: SPR single-cycle kinetics of veligrotug and human IGF-1R interaction. The surface plasmon resonance (SPR) sensorgrams from three independent experiments (blue lines) of the response (resonance units) versus time (seconds) of the single cycle kinetics were performed by injecting five increasing concentrations (6.3, 12.5, 25, 50, and 100 nM) of human His-tagged IGF-1R extracellular domain protein over the veligrotug captured on the Biacore chip surface. The black curves overlaid on the experimental data were obtained by fitting the sensorgram with the 1:1 interaction model. The results demonstrated that veligrotug binds with high affinity to human IGF-1R, with a mean K D value of 0.55 nM, averaged from three independent experiments (range from 0.38–0.69 nM).

Article Snippet: The surface plasmon resonance (SPR) sensorgrams from three independent experiments (blue lines) of the response (resonance units) versus time (seconds) of the single cycle kinetics were performed by injecting five increasing concentrations (6.3, 12.5, 25, 50, and 100 nM) of human His-tagged IGF-1R extracellular domain protein over the veligrotug captured on the Biacore chip surface.

Techniques: SPR Assay

Journal: Journal of Chemical Information and Modeling

Article Title: Active Learning-Guided Hit Optimization for the Leucine-Rich Repeat Kinase 2 WDR Domain Based on In Silico Ligand-Binding Affinities

doi: 10.1021/acs.jcim.5c00588

Figure Lengend Snippet: Experimentally measured binding properties of hit molecules. SPR sensorgrams, fragments (see Figure S2 for full spectra) of NMR spectra of fluorinated compounds (10 μM compound with 0 [black], 20 [red] μM protein), and chemical structures are shown. Solubility and aggregation of compounds as measured by DLS, as well as the set from which each compound was identified, are indicated.

Article Snippet: Eleven hit candidates were advanced to dose–response experiments, eight of which had measurable dissociation constant K D better than 250 μM and acceptable SPR sensorgrams (Chi 2 < 10% R max ; T ( K D ) > 1), with K D values ranging from 18 to 230 μM ( and Table S1 ).

Techniques: Binding Assay, Solubility