Analysis of protein-protein interactions in a complex environment: capture of an analyte-receptor complex with standard additions of the receptor (CARSAR) approach

Analyst. 2012 Aug 21;137(16):3767-72. doi: 10.1039/c2an16217b. Epub 2012 Jun 29.

Abstract

Traditional methods of analytical chemistry to detect an interaction between certain proteins in multicomponent mixtures (e.g. cell lysates, etc.) have limitations. This is due to difficulties in identification of a specific signal of an analyte (a molecule to be detected) against the background. In the present work, we propose the new analytical protocol for transducer-based sensors with a restricted sensitive area. It uses a combination of analyte-receptor complex precipitation with serial additions of the receptor (CARSAR). To test this new analytical strategy, we used a surface plasmon resonance technique to confirm an interaction between the Epstein-Barr virus-encoded nuclear antigen 6 and the mitochondrial ribosomal protein MRPS18-2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Epstein-Barr Virus Nuclear Antigens / metabolism
  • Protein Binding
  • Ribosomal Proteins / metabolism
  • Surface Plasmon Resonance / methods*

Substances

  • Epstein-Barr Virus Nuclear Antigens
  • Ribosomal Proteins