The mechanical properties of single fibrin fibers

J Thromb Haemost. 2010 May;8(5):1030-6. doi: 10.1111/j.1538-7836.2010.03745.x. Epub 2010 Jan 17.


Summary background: Blood clots perform the mechanical task of stemming the flow of blood.

Objectives: To advance understanding and realistic modeling of blood clot behavior we determined the mechanical properties of the major structural component of blood clots, fibrin fibers.

Methods: We used a combined atomic force microscopy (AFM)/fluorescence microscopy technique to determine key mechanical properties of single crosslinked and uncrosslinked fibrin fibers.

Results and conclusions: Overall, full crosslinking renders fibers less extensible, stiffer, and less elastic than their uncrosslinked counterparts. All fibers showed stress relaxation behavior (time-dependent weakening) with a fast and a slow relaxation time, 2 and 52 s. In detail, crosslinked and uncrosslinked fibrin fibers can be stretched to 2.5 and 3.3 times their original length before rupturing. Crosslinking increased the stiffness of fibers by a factor of 2, as the total elastic modulus, E(0), increased from 3.9 to 8.0 MPa and the relaxed, elastic modulus, E(infinity), increased from 1.9 to 4.0 MPa upon crosslinking. Moreover, fibers stiffened with increasing strain (strain hardening), as E(0) increased by a factor of 1.9 (crosslinked) and 3.0 (uncrosslinked) at strains epsilon > 110%. At low strains, the portion of dissipated energy per stretch cycle was small (< 10%) for uncrosslinked fibers, but significant (approximately 40%) for crosslinked fibers. At strains > 100%, all fiber types dissipated about 70% of the input energy. We propose a molecular model to explain our data. Our single fiber data can now also be used to construct a realistic, mechanical model of a fibrin network.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Biomechanical Phenomena
  • Fibrin / physiology*
  • Humans
  • Microscopy, Atomic Force
  • Microscopy, Fluorescence


  • Fibrin