Multiscale Mechanics of Fibrin Polymer: Gel Stretching with Protein Unfolding and Loss of Water

Blood clots and thrombi consist primarily of a mesh of branched fibers made of the protein fibrin. We propose a molecular basis for the marked extensibility and negative compressibility of fibrin gels based on the structural and mechanical properties of clots at the network, fiber, and molecular lev...

Full description

Saved in:
Bibliographic Details
Published inScience (American Association for the Advancement of Science) Vol. 325; no. 5941; pp. 741 - 744
Main Authors Brown, André E.X, Litvinov, Rustem I, Discher, Dennis E, Purohit, Prashant K, Weisel, John W
Format Journal Article
LanguageEnglish
Published Washington, DC American Association for the Advancement of Science 07.08.2009
The American Association for the Advancement of Science
Subjects
Biological and medical sciences
Biopolymers - chemistry
Blood clots
Blood Coagulation
Bundling
Compressibility
Data lines
Fibrin - chemistry
Fibrinogen - chemistry
Fracture mechanics
Fundamental and applied biological sciences. Psychology
Gels
Humans
Mechanical Phenomena
Mechanical properties
Microscopy, Electron
Miscellaneous
Models, Molecular
Molecular biology
Molecular biophysics
Molecules
Physico-chemical properties of biomolecules
Polymers
Protein Folding
Protein unfolding
Proteins
Rubber
Sprains and strains
Stress, Mechanical
Water - chemistry
Water
Blood coagulation
Fibrin
Thrombus
Unfolding
Polymer
Stretching
Protein
Online AccessGet full text

Cover

More Information
Summary:Blood clots and thrombi consist primarily of a mesh of branched fibers made of the protein fibrin. We propose a molecular basis for the marked extensibility and negative compressibility of fibrin gels based on the structural and mechanical properties of clots at the network, fiber, and molecular levels. The force required to stretch a clot initially rises linearly and is accompanied by a dramatic decrease in clot volume and a peak in compressibility. These macroscopic transitions are accompanied by fiber alignment and bundling after forced protein unfolding. Constitutive models are developed to integrate observations at spatial scales that span six orders of magnitude and indicate that gel extensibility and expulsion of water are both manifestations of protein unfolding, which is not apparent in other matrix proteins such as collagen.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1172484