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A Comparison of the Mechanical and Structural Properties of Fibrin Fibers with Other Protein Fibers

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Abstract

In the past few years a great deal of progress has been made in studying the mechanical and structural properties of biological protein fibers. Here, we compare and review the stiffness (Young’s modulus, E) and breaking strain (also called rupture strain or extensibility, εmax) of numerous biological protein fibers in light of the recently reported mechanical properties of fibrin fibers. Emphasis is also placed on the structural features and molecular mechanisms that endow biological protein fibers with their respective mechanical properties. Generally, stiff biological protein fibers have a Young’s modulus on the order of a few Gigapascal and are not very extensible (εmax < 20%). They also display a very regular arrangement of their monomeric units. Soft biological protein fibers have a Young’s modulus on the order of a few Megapascal and are very extensible (εmax > 100%). These soft, extensible fibers employ a variety of molecular mechanisms, such as extending amorphous regions or unfolding protein domains, to accommodate large strains. We conclude our review by proposing a novel model of how fibrin fibers might achieve their extremely large extensibility, despite the regular arrangement of the monomeric fibrin units within a fiber. We propose that fibrin fibers accommodate large strains by two major mechanisms: (1) an α-helix to β-strand conversion of the coiled coils; (2) a partial unfolding of the globular C-terminal domain of the γ-chain.

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Acknowledgments

We thank M. C. Stahle, J. L. Moen, and O. V. Gorkun for advice and technical assistance. We acknowledge support from NIH: P41 EB002025 (RS), R01 HL31048 (STL), R41 CA103120 (MG); NSF: CMMI-0646627 (MG); Research Corporation: RI0826 (MG); American Cancer Society: IRG-93-035-6 (MG) and the American Heart Association, Mid-Atlantic Affiliate Grant-in-Aid 055527U (RRH).

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Authors and Affiliations

  1. Department of Physics, Wake Forest University, Winston-Salem, NC, 27109, USA

    M. Guthold, W. Liu, E. A. Sparks & L. Peng

  2. Department of Physics, Harvard University, Cambridge, MA, 02138, USA

    L. M. Jawerth

  3. Curriculum in Applied and Materials Science, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA

    M. Falvo

  4. Department of Physics and Astronomy, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA

    R. Superfine

  5. Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem, NC, 27157, USA

    R. R. Hantgan

  6. Department of Pathology and Laboratory Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA

    S. T. Lord

Authors
  1. M. Guthold
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  2. W. Liu
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  3. E. A. Sparks
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  4. L. M. Jawerth
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  5. L. Peng
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  6. M. Falvo
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  7. R. Superfine
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  8. R. R. Hantgan
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  9. S. T. Lord
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Corresponding author

Correspondence to M. Guthold.

Additional information

The senior authors R. R. Hantgan and S. T. Lord have contributed equally to this article.

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Guthold, M., Liu, W., Sparks, E.A. et al. A Comparison of the Mechanical and Structural Properties of Fibrin Fibers with Other Protein Fibers. Cell Biochem Biophys 49, 165–181 (2007). https://doi.org/10.1007/s12013-007-9001-4

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  • DOI: https://doi.org/10.1007/s12013-007-9001-4

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