Kinetics of the multistep rupture of fibrin 'A-a' polymerization interactions measured using atomic force microscopy.

ABSTRACT: Fibrin, the structural scaffold of blood clots, spontaneously polymerizes through the formation of 'A-a' knob-hole bonds. When subjected to external force, the dissociation of this bond is accompanied by two to four abrupt changes in molecular dimension observable as rupture events in a force curve. Herein, the configuration, molecular extension, and kinetic parameters of each rupture event are examined. The increases in contour length indicate that the D region of fibrinogen can lengthen by approximately 50% of the length of a fibrin monomer before rupture of the 'A-a' interaction. The dependence of the dissociation rate on applied force was obtained using probability distributions of rupture forces collected at different pull-off velocities. These distributions were fit using a model in

SUBMITTER: Averett LE 

PROVIDER: S-EPMC2776257 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature