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Protein unfolding accounts for the unusual mechanical behavior of fibrin networks

Paper ID Volume ID Publish Year Pages File Format Full-Text
1343 82 2011 10 PDF Available
Title
Protein unfolding accounts for the unusual mechanical behavior of fibrin networks
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.

Keywords
Blood clots; Poisson’s ratio; Constitutive model; Viscoelasticity; Nanomechanics
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Protein unfolding accounts for the unusual mechanical behavior of fibrin networks
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Publisher
Database: Elsevier - ScienceDirect
Journal: Acta Biomaterialia - Volume 7, Issue 6, June 2011, Pages 2374–2383
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us