Our WAVEsystem has been presented in the following posters
A physicochemical approach to characterizing antibody-drug conjugates through stability into target validation
PEGSBoston Virtual 2020 - Waters & Collaborators
A panel of methods were used to establish comprehensive characterization of antibody-drug conjugates (ADCs), including liquid chromatography, mass spectrometry, size exclusion chromatography, microfluidic modulation spectroscopy, differential scanning calorimetry, grating-coupled interferometry (GCI) and isothermal titration calorimetry.
Spotting the weakest binders
Reliably determine off-rates of up to 10s-1, starting with just a crude reaction mixture. Work with a wide variety of solvents - including acetonitrile and high concentrations of DMSO - and minimize the occurrence of false positives.
Keeping kinetics real
PEGS Europe 2019
Kinetic characterization of analytes binding to membrane proteins (GPCRs) embedded in virus-like particles (VLPs) and captured from crude cell membrane extracts (centrifugation-sonication).
Real samples, real data
PEGS Europe 2019
Assess antibody profiling in undiluted biofluids for reliable kinetic profiling in conditions closer to real life. Study kinetics in aggregating proteins (fibrils).
Full kinetic characterization of antibodies in biofluids
Immunotherapies and Innovations for Infectious Diseases 2019
Assess antibody profiling in undiluted serum, measure kinetics in plasma and quantify anti-drug-antibody (ADA) titers directly from blood serum.
GCI: a new method for label-free protein interaction studies
Plants, Peptides and Receptors in Málaga 2018
Here we characterize the interactions of various plant leucine-rich repeat receptor kinases (LRR-RKs) with their cognate ligands and SERK-family co-receptors using a label-free surface biosensor based on grating-coupled interferometry (GCI). Due to the comparably low amount of recombinant protein and analyte needed, GCI is an excellent alternative for experiments where key components are scarce.
Discovery of CLIPS binders to anti-TNFa mAb’s using phage display libraries
Presented by Pepscan
Here we report the use of a monocyclic phage library encoding for a fully randomized 10-
mer peptide sequence flanked by two cysteines that are linked via a CLIPSTM scaffold to identify peptide binders that bind to Infliximab. Binding assessed with the WAVEsystem.
Augmented affinity in antibody-antigen interactions: impact on design of diagnostic assays
Presented by Mologic at PEGS Boston 2019
Anti-p24 antibody binding kinetics were measured using the Creoptix WAVEdelta system. The results of this study reveal a surprising enhancement in affinity due to a significant 21-fold increase in on-rate when anti-p24 mAb1 recognizes the anti-p24 mAb2-p24 complex.