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Science 4 August 2006:
Vol. 313. no. 5787, p. 634
DOI: 10.1126/science.1127317
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Brevia

Fibrin Fibers Have Extraordinary Extensibility and Elasticity

W. Liu,1* L. M. Jawerth,2* E. A. Sparks,1 M. R. Falvo,3 R. R. Hantgan,6 R. Superfine,4 S. T. Lord,5{dagger} M. Guthold1{dagger}

Blood clots perform an essential mechanical task, yet the mechanical behavior of fibrin fibers, which form the structural framework of a clot, is largely unknown. By using combined atomic force-fluorescence microscopy, we determined the elastic limit and extensibility of individual fibers. Fibrin fibers can be strained 180% (2.8-fold extension) without sustaining permanent lengthening, and they can be strained up to 525% (average 330%) before rupturing. This is the largest extensibility observed for protein fibers. The data imply that fibrin monomers must be able to undergo sizeable, reversible structural changes and that deformations in clots can be accommodated by individual fiber stretching.

1 Department of Physics, Wake Forest University, Winston-Salem, NC 27109, USA.
2 Department of Physics, Harvard University, Cambridge, MA 02138, USA.
3 Curriculum in Applied and Materials Science, University of North Carolina, Chapel Hill, NC 27599, USA.
4 Department of Physics and Astronomy, University of North Carolina, Chapel Hill, NC 27599, USA.
5 Department of Pathology and Laboratory Medicine, University of North Carolina, Chapel Hill, NC 27599, USA.
6 Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem, NC 27157, USA.

* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: gutholdm{at}wfu.edu (M.G.); stl{at}med.unc.edu (S.T.L.)

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Forced Unfolding of Coiled-Coils in Fibrinogen by Single-Molecule AFM.
A. E. X. Brown, R. I. Litvinov, D. E. Discher, and J. W. Weisel (2007)
Biophys. J. 92, L39-L41
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Science. ISSN 0036-8075 (print), 1095-9203 (online)