title: Biophysical methods for the determination of antibody-antigen affinities.
abstract: Binding specificities against virtually any antigen can be isolated from antibody libraries displayed on filamentous phage. The determination of antibody-antigen affinity constants and binding kinetics is an important part of antibody characterization, and may be predictive of antibody performance in biotechnological applications. This article, intended as a guideline for the scientist who isolates a novel antibody and wishes to characterize its binding properties, presents the authors' view on widely used methodologies for the quantitative determination of antibody-antigen interactions.
authors.affiliation: Institute of Molecular Biology and Biophysics, ETH Hoenggerberg, Zürich, Switzerland. dario@mol.biol.ethz.ch
authors.forename: D
authors.initials: D
authors.lastname: Neri
authors.forename: S
authors.initials: S
authors.lastname: Montigiani
authors.forename: P M
authors.initials: PM
authors.lastname: Kirkham
mesh_terms: D000915:Antibody Affinity; D000937:Antigen-Antibody Reactions; D055592:Biophysical Phenomena; D001703:Biophysics; D001709:Biotechnology; D007700:Kinetics