Nanomolar to sub-picomolar affinity measurements of antibody-antigen interactions and protein multimerizations: fluorescence-assisted high-performance liquid chromatography

Anal Biochem. 2013 Jun 15;437(2):118-22. doi: 10.1016/j.ab.2013.02.027. Epub 2013 Mar 13.

Abstract

Although several techniques exist for the measurement of high-affinity interactions, it is still challenging to determine dissociation constants around or even below 1pM. During the analysis of several human-derived monoclonal antibodies to adalimumab, we found a clone with a very high affinity that could not be measured using conventional surface plasmon resonance assays. We developed a straightforward and robust method to measure affinities in the nanomolar to sub-picomolar range. The assay is based on separation of bound and free fluorescently labeled antigen using size exclusion chromatography and quantification by in-line fluorescence detection. We describe optimal conditions and procedures that result in a very sensitive assay that can be used to reliably determine ultra-high affinities. Using the method described in this article, a dissociation constant of 0.78pM could be determined for the anti-adalimumab antibody.

MeSH terms

  • Adalimumab
  • Antibodies / chemistry
  • Antibodies / physiology*
  • Antibodies, Monoclonal, Humanized / immunology*
  • Antibodies, Monoclonal, Humanized / therapeutic use
  • Antibody Affinity / physiology*
  • Antirheumatic Agents / therapeutic use
  • Arthritis, Rheumatoid / drug therapy
  • B-Lymphocytes / metabolism
  • Chromatography, High Pressure Liquid / methods*
  • Fluorescence
  • Humans
  • Interleukin-6 / immunology
  • Sensitivity and Specificity
  • Tetanus Toxoid / immunology

Substances

  • Antibodies
  • Antibodies, Monoclonal, Humanized
  • Antirheumatic Agents
  • Interleukin-6
  • Tetanus Toxoid
  • Adalimumab