Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Acta Biomater. 2011 Jun;7(6):2374-83. doi: 10.1016/j.actbio.2011.02.026. Epub 2011 Feb 20.

Protein unfolding accounts for the unusual mechanical behavior of fibrin networks.

Author information

  • 1Department of Mechanical Engineering and Applied Mechanics, University of Pennsylvania, Philadelphia, PA 19104, USA.

Abstract

We describe the mechanical behavior of isotropic fibrin networks at the macroscopic scale in terms of the nanoscale force response of fibrin molecules that are its basic building blocks. We show that the remarkable extensibility and compressibility of fibrin networks have their origins in the unfolding of fibrin molecules. The force-stretch behavior of a single fibrin fiber is described using a two-state model in which the fiber has a linear force-stretch relation in the folded phase and behaves like a worm-like-chain in the unfolded phase. The nanoscale force-stretch response is connected to the macro-scale stress-stretch response by means of the eight-chain model. This model is able to capture the macroscopic response of a fibrin network in uniaxial tension and appears remarkably simple given the molecular complexity. We use the eight-chain model to explain why fibrin networks have negative compressibility and Poisson's ratio greater than 1 due to unfolding of fibrin molecules.

Copyright © 2011 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.

PMID:
21342665
[PubMed - indexed for MEDLINE]
PMCID:
PMC3134297
Free PMC Article

Images from this publication.See all images (9)Free text

Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
Figure 7
Figure 8
Figure 9
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Write to the Help Desk