Peptides represent a unique class of pharmaceutical compounds, molecularly poised between small molecules and proteins, yet biochemically and therapeutically distinct from both. Given their attractive pharmacological profile and intrinsic properties, peptides represent an excellent starting point for the design of novel therapeutics and their specificity has been seen to translate into excellent safety, tolerability, and efficacy profiles in humans.
Surface plasmon resonance (SPR) is a useful biosensor technique for the study of biomolecular interactions, with the potential for high-throughput screening of ligand interactions with drug targets. Typically, one of the binding partners is immobilized on the surface and the binding partner can flow over the top. SPR allows for the real-time measurement of binding, thus providing kinetic information and is also highly sensitive. SPR has many advantages over other techniques used to study bimolecular interactions such as ITC, including low consumption of material due to the micro-fluidic design of the instruments.
The technique affords numerous ways of immobilizing biomolecules to the surface, including amine coupling, biotin capture and capture using antibodies. In addition, potentially either binding partner can be immobilized to the surface. Here at Seattle Genova, we provide affinity and kinetics analysis for therapeutic peptides with both BLI and SPR technologies.
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