Hepatitis B surface antigen-antibody interactions studied by optical tweezers

IET Nanobiotechnol. 2012 Mar;6(1):9-15. doi: 10.1049/iet-nbt.2010.0023.

Abstract

The protein-protein interactions between hepatitis B surface antigen (HBsAg) and its antibodies (anti-HBs) were studied by measuring the binding force between microspheres coated with such proteins using optical tweezers. The interaction force between the protein-coated microspheres was found to be strongly influenced by the acidity of the surrounding liquid medium, as well as the experimental temperature, and it reaches a maximum value at around pH 7.5 and temperature around 37°C. By measuring the protein distribution on the surfaces of the microspheres and their contact areas using scanning electron microscopy, the specific binding force between an HBsAg and anti-HBs protein pair is estimated to be around 4.8 pN at the optimum pH value and temperature at an applied loading rate of around 1 pN/s.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigen-Antibody Complex / chemistry*
  • Hepatitis B Antibodies / chemistry*
  • Hepatitis B Antibodies / immunology*
  • Hepatitis B Surface Antigens / chemistry*
  • Hepatitis B Surface Antigens / immunology*
  • Optical Tweezers*
  • Protein Binding

Substances

  • Antigen-Antibody Complex
  • Hepatitis B Antibodies
  • Hepatitis B Surface Antigens