A comparison of binding surfaces for SPR biosensing using an antibody-antigen system and affinity distribution analysis.

ABSTRACT: The application of optical biosensors in the study of macromolecular interactions requires immobilization of one binding partner to the surface. It is often highly desirable that the immobilization is uniform and does not affect the thermodynamic and kinetic binding parameters to soluble ligands. To achieve this goal, a variety of sensor surfaces, coupling strategies and surface chemistries are available. Previously, we have introduced a technique for determining the distribution of affinities and kinetic rate constants from families of binding and dissociation traces acquired at different concentrations of soluble ligand. In the present work, we explore how this affinity distribution analysis can be useful in the assessment and optimization of surface immobilization. With this goal, using

SUBMITTER: Zhao H 

PROVIDER: S-EPMC3840496 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature