Mechanical Distortion of Protein Receptor Decreases the Lifetime of a Receptor−Ligand Bond
Author(s) -
Senli Guo,
Nan Li,
Nimit Lad,
Chad Ray,
Boris B. Akhremitchev
Publication year - 2010
Publication title -
journal of the american chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.115
H-Index - 612
eISSN - 1520-5126
pISSN - 0002-7863
DOI - 10.1021/ja1011756
Subject(s) - chemistry , dissociation rate , dissociation (chemistry) , covalent bond , molecule , chemical physics , molecular dynamics , biophysics , force spectroscopy , receptor , streptavidin , nanotechnology , computational chemistry , crystallography , biotin , biochemistry , materials science , organic chemistry , biology
Substantial experimental evidence indicates that the mechanical force applied to pull apart non-covalent molecular bonds (such as receptor-ligand pairs) can significantly decrease the bond lifetime. This evidence is often generated in single-molecule experiments that are designed to specifically test effects of pulling forces. However, the effect of compressive forces on the lifetime of receptor-ligand bonds remains largely unexplored. Here we extend the common usage of the atomic force microscopy technique to study whether compressive forces applied to bound streptavidin-biotin species can significantly accelerate the rate of dissociation. Presented experimental data indicate that compressive forces can substantially decrease the lifetime of the molecular bond. Surprisingly, the efficiency of accelerating dissociation by compressive forces sometimes exceeds the enhancement of the dissociation rate measured in pulling experiments, indicating that compressive forces applied to the bound species might be efficiently used to control the lifetime of adhesion bonds.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom