Influence of bovine and human serum albumin on the binding kinetics of biomolecular interactions
Benjamin Charron, Alexandre Delorme, Caroline Dubois, Maryam Hojjat Jodaylami, Jean‐François Masson
Abstract
conditions. We also clearly demonstrate why a minimum dilution of 1 : 10 is often required in SPR assays to remove most background effects. Taken together, these results show that: (1) BSA does not affect the binding constant between antibodies and thus serves its purpose well when only surface blocking is intended, (2) HSA is an adequate surrogate for human serum in assay optimization, and (3) blocking buffers should be prepared with HSA in the optimization steps of assays to be translated to human blood or serum.
Topics & Concepts
Bovine serum albuminKineticsHuman serum albuminChemistrySerum albuminHuman albuminReceptor–ligand kineticsPlasma protein bindingBiosensorAlbuminChromatographyBiochemistryReceptorQuantum mechanicsPhysicsProtein Interaction Studies and Fluorescence AnalysisMonoclonal and Polyclonal Antibodies ResearchAdvanced Biosensing Techniques and Applications