Multiscale mechanics of fibrin polymer: gel stretching with protein unfolding and loss of water.

Full Abstract

Blood clots and thrombi consist primarily of a mesh of branched fibers made of the protein fibrin. We propose a molecular basis for the marked extensibility and negative compressibility of fibrin gels based on the structural and mechanical properties of clots at the network, fiber, and molecular levels. The force required to stretch a clot initially rises linearly and is accompanied by a dramatic decrease in clot volume and a peak in compressibility. These macroscopic transitions are accompanied by fiber alignment and bundling after forced protein unfolding. Constitutive models are developed to integrate observations at spatial scales that span six orders of magnitude and indicate that gel extensibility and expulsion of water are both manifestations of protein unfolding, which is not apparent in other matrix proteins such as collagen.

Author information

Author/s: Brown, André E X (AE); Litvinov, Rustem I (RI); Discher, Dennis E (DE); Purohit, Prashant K (PK); Weisel, John W (JW);

Affiliation: Department of Physics and Astronomy, University of Pennsylvania, Philadelphia, PA 19104, USA.

Grants: HL090774 (Agency:NHLBI NIH HHS) ; HL30954 (Agency:NHLBI NIH HHS) ; HL62352 (Agency:NHLBI NIH HHS)

Journal and publication information

Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.

Journal: Science (New York, N.Y.) (Science), published in United States. (Language: eng)

Reference: 2009-Aug; vol 325 (issue 5941) : pp 741-4

Dates: Created 2009/08/07; Completed 2009/08/20;

PMID: 19661428, status: MEDLINE (last retrieved date: 8/21/2009)

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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