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Biophys J ; 79(3): 1206-12, 2000 Sep.
Article in English | MEDLINE | ID: mdl-10968985

ABSTRACT

We discuss models for the force-induced dissociation of a ligand-receptor bond, occurring in the context of cell adhesion or single molecule unbinding force measurements. We consider a bond with a structured energy landscape which is modeled by a network of force dependent transition rates between intermediate states. The behavior of a model with only one intermediate state and a model describing a molecular zipper is studied. We calculate the bond lifetime as a function of an applied force and unbinding forces under an increasing applied load and determine the relationship between both quantities. The dissociation via an intermediate state can lead to distinct functional relations of the bond lifetime on force. One possibility is the occurrence of three force regimes where the lifetime of the bond is determined by different transitions within the energy landscape. This case can be related to recent experimental observations of the force-induced dissociation of single avidin-biotin bonds.


Subject(s)
Ligands , Models, Theoretical , Receptors, Cell Surface/chemistry , DNA/chemistry , Kinetics , Nucleic Acid Conformation , Protein Binding , Protein Conformation , Receptors, Cell Surface/metabolism , Stress, Mechanical , Thermodynamics
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