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Microscale spatial heterogeneity of protein structural transitions in fibrin matrices

Following an injury, a blood clot must form at the wound site to stop bleeding before skin repair can occur. Blood clots must satisfy a unique set of material requirements; they need to be sufficiently strong to resist pressure from the arterial blood flow but must be highly flexible to support larg...

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Autores principales: Fleissner, Frederik, Bonn, Mischa, Parekh, Sapun H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Association for the Advancement of Science 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5566164/
https://www.ncbi.nlm.nih.gov/pubmed/28861472
http://dx.doi.org/10.1126/sciadv.1501778
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author Fleissner, Frederik
Bonn, Mischa
Parekh, Sapun H.
author_facet Fleissner, Frederik
Bonn, Mischa
Parekh, Sapun H.
author_sort Fleissner, Frederik
collection PubMed
description Following an injury, a blood clot must form at the wound site to stop bleeding before skin repair can occur. Blood clots must satisfy a unique set of material requirements; they need to be sufficiently strong to resist pressure from the arterial blood flow but must be highly flexible to support large strains associated with tissue movement around the wound. These combined properties are enabled by a fibrous matrix consisting of the protein fibrin. Fibrin hydrogels can support large macroscopic strains owing to the unfolding transition of α-helical fibril structures to β sheets at the molecular level, among other reasons. Imaging protein secondary structure on the submicrometer length scale, we reveal that another length scale is relevant for fibrin function. We observe that the protein polymorphism in the gel becomes spatially heterogeneous on a micrometer length scale with increasing tensile strain, directly showing load-bearing inhomogeneity and nonaffinity. Supramolecular structural features in the hydrogel observed under strain indicate that a uniform fibrin hydrogel develops a composite-like microstructure in tension, even in the absence of cellular inclusions.
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spelling pubmed-55661642017-08-31 Microscale spatial heterogeneity of protein structural transitions in fibrin matrices Fleissner, Frederik Bonn, Mischa Parekh, Sapun H. Sci Adv Research Articles Following an injury, a blood clot must form at the wound site to stop bleeding before skin repair can occur. Blood clots must satisfy a unique set of material requirements; they need to be sufficiently strong to resist pressure from the arterial blood flow but must be highly flexible to support large strains associated with tissue movement around the wound. These combined properties are enabled by a fibrous matrix consisting of the protein fibrin. Fibrin hydrogels can support large macroscopic strains owing to the unfolding transition of α-helical fibril structures to β sheets at the molecular level, among other reasons. Imaging protein secondary structure on the submicrometer length scale, we reveal that another length scale is relevant for fibrin function. We observe that the protein polymorphism in the gel becomes spatially heterogeneous on a micrometer length scale with increasing tensile strain, directly showing load-bearing inhomogeneity and nonaffinity. Supramolecular structural features in the hydrogel observed under strain indicate that a uniform fibrin hydrogel develops a composite-like microstructure in tension, even in the absence of cellular inclusions. American Association for the Advancement of Science 2016-07-08 /pmc/articles/PMC5566164/ /pubmed/28861472 http://dx.doi.org/10.1126/sciadv.1501778 Text en Copyright © 2016, The Authors http://creativecommons.org/licenses/by-nc/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (http://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited.
spellingShingle Research Articles
Fleissner, Frederik
Bonn, Mischa
Parekh, Sapun H.
Microscale spatial heterogeneity of protein structural transitions in fibrin matrices
title Microscale spatial heterogeneity of protein structural transitions in fibrin matrices
title_full Microscale spatial heterogeneity of protein structural transitions in fibrin matrices
title_fullStr Microscale spatial heterogeneity of protein structural transitions in fibrin matrices
title_full_unstemmed Microscale spatial heterogeneity of protein structural transitions in fibrin matrices
title_short Microscale spatial heterogeneity of protein structural transitions in fibrin matrices
title_sort microscale spatial heterogeneity of protein structural transitions in fibrin matrices
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5566164/
https://www.ncbi.nlm.nih.gov/pubmed/28861472
http://dx.doi.org/10.1126/sciadv.1501778
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