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: 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: Methods in Molecular Biology™

Article Title: DNA-Protein Interactions

doi: 10.1007/978-1-60327-015-1

Figure Lengend Snippet: Fig. 2. Sensorgram showing the different steps of the immobilisation of DNA on an SA-5 sensor chip. Phase 1 : drop in signal as NaOH is passed over the sensor chip surface. A new baseline signal (a) is reached at the end of this injection due to the loss of loosely bound streptavidin from the surface. Phase 2 : injection and binding of biotinylated DNA to the surface. At the end of this injection an increased baseline signal is seen (b), due to the bound DNA. Phase 3 : injection of SDS to remove loosely bound DNA from the surface of the sensor chip. At the end of this injection a slightly lowered baseline signal is established (c). If the baseline signal, a, is subtracted from this new reading, c, the amount of DNA immobilised onto the surface can be calculated (1).

Article Snippet: The interaction between molecules in BIAcore is monitored over time and presented as a sensorgram, i.e. a plot of response units (RU) versus time (s).

Techniques: Injection, Binding Assay

Journal: Methods in Molecular Biology™

Article Title: DNA-Protein Interactions

doi: 10.1007/978-1-60327-015-1

Figure Lengend Snippet: Fig. 3. ( a ). A typical sensorgram showing MetJ binding to and dissociating from the operator-derivatised sensor chip sur- face and the regeneration of the sensor chip. Phase 1 : initial baseline signal when running buffer passes over the sensor chip. Phase 2 : first injection containing MetJ and AdoMet. The change in signal is due to the binding of the holo-repressor to the chip surface. Phase 3 : second injection of running buffer containing AdoMet alone, allowing the dissociation in the presence of effector to be measured. Phase 4 : regeneration of the sensor chip surface by the injection of SDS (1).

Article Snippet: The interaction between molecules in BIAcore is monitored over time and presented as a sensorgram, i.e. a plot of response units (RU) versus time (s).

Techniques: Binding Assay, Injection

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