Inner complexity of molecular adhesion bonds

Abstract

Weak noncovalent interactions between large molecules sustain most of cell structure and interfacial adhesion in biology. Because of thermal activation, these bonds have modest lifetimes and the lifetimes are progressively shortened under application of force. Theory shows that the dynamic spectrum of most frequent force versus log(loading rate) from bond breakage tests images the prominent energy barriers traversed along the molecular unbinding pathway, which establishes a direct link between measurements of force and bond chemistry. Applied to bioadhesion bonds and membrane cohesion, dynamic force spectroscopy provides a new level of insight into the complexity of macromolecular interactions and exposes the unexpected impact of force on biochemical kinetics.