Single-molecule avidin-biotin association reaction studied by force-clamp spectroscopy

Ultramicroscopy. 2008 Sep;108(10):1135-9. doi: 10.1016/j.ultramic.2008.04.058. Epub 2008 May 14.

Abstract

Using single-molecule force-clamp spectroscopy, where the distance between the AFM tip and the sample surface is fixed and a few parallel avidin-biotin complexes are kept stretched by a certain force, we were able to observe the formation of single avidin-biotin bonds. Perspectives to use such an approach to study association reactions at single-molecule level in the conditions resembling those characteristic for some processes in vivo (e.g. virus-cell membrane attachment) are briefly discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Avidin* / chemistry
  • Avidin* / metabolism
  • Biotin* / chemistry
  • Biotin* / metabolism
  • Cattle
  • Microscopy, Atomic Force / methods*
  • Spectrum Analysis / methods*

Substances

  • Avidin
  • Biotin