Dynamic disorder in receptor-ligand forced dissociation experiments.
Recently experiments showed that some biological noncovalent bonds increase their lifetimes when they are stretched by an external force, and their lifetimes will decrease when the force increases further. Several specific quantitative models have been proposed to explain the intriguing transitions from the "catch bond" to the "slip bond." In this work we propose that the dynamic disorder of the force-dependent dissociation rate can account for the counterintuitive behaviors of the bonds. A Gaussian stochastic rate model is used to quantitatively describe the transitions observed recently in the single bond P-selctin glycoprotein ligand 1-P-selectin force rupture experiment [Marshall, Nature 423, 190 (2003)]. Our model agrees well with the experimental data. We conclude that the catch bonds could arise from the stronger positive correlation between the height of the intrinsic energy barrier and the distance from the bound state to the barrier; classical pathway scenario or a priori catch bond assumption is not essential.
Liu
Fei
F
Center for Advanced Study, Tsinghua University, Beijing 100084, China. liufei@tsinghua.edu.cn
Ou-Yang
Zhong-can
ZC
Iwamoto
Mitsumasa
M
D001703:Biophysics / Q000379:methods*; D019281:Dimerization; D007700:Kinetics; D008024:Ligands; D015233:Models, Statistical; D016011:Normal Distribution; D011485:Protein Binding; D019087:Selectins; D013269:Stochastic Processes; D013816:Thermodynamics
D008024:Ligands; D019087:Selectins