Single-molecule avidin-biotin association reaction studied by force-clamp spectroscopy.
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.
Favre
Mélanie
M
Laboratoire de Physique de la Matière Vivante, IPMC, BSP, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland. melanie.favre@epfl.ch
Sekatskii
Serguei K
SK
Dietler
Giovanni
G
D000818:Animals; D001360:Avidin / Q000737:chemistry / Q000378:metabolism; D001710:Biotin / Q000737:chemistry / Q000378:metabolism; D002417:Cattle; D018625:Microscopy, Atomic Force / Q000379:methods*; D013057:Spectrum Analysis / Q000379:methods*
D001360:Avidin; D001710:Biotin