Force spectroscopy of the fibrin(ogen)–fibrinogen interaction

Abstract

Fibrin aggregation is of vital importance in many physiological and pathological processes, such as blood coagulation, wound healing, and thrombosis. In the present study, we investigated the forces involved in the initial steps of the fibrinogen fibrin aggregation by force spectroscopy using the atomic force microscope. Our data confirm the existence of strong specific interactions between fibrin and fibrin(ogen), with unbinding forces ranging from 290 to 375 pN and a logarithmic dependence on the loading rate between 0.8 and 23 nN/s. © 2007 Wiley Periodicals, Inc. Biopolymers 89: 292–301, 2008. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

Variations on Fibrinogen-Erythrocyte Interactions during Cell Aging

“…The protein-AFM tips functionalization process has been described elsewhere [8], [15], [16]. Briefly, cleaned AFM silicon nitride tips were silanized with 3-aminopropyl-triethoxysilane (APTES) for 1 h in argon atmosphere.…”

Fibrin gels and their clinical and bioengineering applications

“…Recent studies by atomic force microscopy have shown that stretching and limited unfolding of fibrin monomers occur at lower forces (Brown et al 2007) than those required to detach a fibrin monomer from the lateral bonds holding it within the protofibril (Litvinov et al 2005;Brown et al 2007;Chtcheglova et al 2008).…”

“…The similarity of Young's moduli of fibrin protofibrils and fibres implies that the bonds holding protofibrils together within a fibre are strong enough to prevent protofibril slippage as a fibre is bent, and suggests that the compliance of the fibre comes from longitudinal stretching due to the flexibility of the superhelical coils formed by the three strands in the regions connecting the central and end domains. Recent studies by atomic force microscopy have shown that stretching and limited unfolding of fibrin monomers occur at lower forces (Brown et al 2007) than those required to detach a fibrin monomer from the lateral bonds holding it within the protofibril (Litvinov et al 2005;Brown et al 2007;Chtcheglova et al 2008).…”

Kinetic model of two-monomer polymerization

“…We have previously modeled aspects of fibrin polymerization [13,14], but in these models, we did not account for the fact that fibrinogen can bind with fibrin but not directly with other fibrinogen molecules. Oligomers of mixtures of fibrinogen and fibrin have been observed experimentally [12,[15][16][17], and these experiments suggest that this additional type of reaction affects the kinetics of the overall fibrin gelation process. With the ultimate goal of modeling the fibrin-fibrinogen system, here we look at a simplified model, in the belief that our study of it will usefully inform our analysis of the actual biological system.…”