| Literature DB >> 30196510 |
Stephen Hearty1,2, Paul Leonard1,2, Hui Ma1, Richard O'Kennedy3,4,5.
Abstract
Surface plasmon resonance (SPR) is now widely embraced as a technology for monitoring a diverse range of protein-protein interactions and is considered almost de rigueur for characterizing antibody-antigen interactions. The technique obviates the need to label either of the interacting species, and the binding event is visualized in real time. Thus, it is ideally suited for screening crude, unpurified antibody samples that dominate early candidate panels following antibody selection campaigns. SPR returns not only concentration and affinity data but when used correctly can resolve the discrete component kinetic parameters (association and dissociation rate constants) of the affinity interaction. Herein, we outline some SPR-based generic antibody screening configurations and methodologies in the context of expediting data-rich ranking of candidate antibody panels and ensuring that antibodies with the optimal kinetic binding characteristics are reliably identified.Keywords: Affinity; Antibody; Antigen; Association rate; Dissociation rate; Screening; Surface plasmon resonance (SPR)
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Year: 2018 PMID: 30196510 DOI: 10.1007/978-1-4939-8648-4_22
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745