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Osmotic pressure induced tensile forces in tendon collagen
Water is an important component of collagen in tendons, but its role for the function of this load-carrying protein structure is poorly understood. Here we use a combination of multi-scale experimentation and computation to show that water is an integral part of the collagen molecule, which changes...
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Published in: | Nature communications 2015-01, Vol.6 (1), p.5942-5942, Article 5942 |
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description | Water is an important component of collagen in tendons, but its role for the function of this load-carrying protein structure is poorly understood. Here we use a combination of multi-scale experimentation and computation to show that water is an integral part of the collagen molecule, which changes conformation upon water removal. The consequence is a shortening of the molecule that translates into tensile stresses in the range of several to almost 100 MPa, largely surpassing those of about 0.3 MPa generated by contractile muscles. Although a complete drying of collagen would be relevant for technical applications, such as the fabrication of leather or parchment, stresses comparable to muscle contraction already occur at small osmotic pressures common in biological environments. We suggest, therefore, that water-generated tensile stresses may play a role in living collagen-based materials such as tendon or bone.
Water is an important component of collagen in tendons, bone and extracellular matrix, but its role in the mechanical function of protein is poorly understood. Here, the authors study the effects of osmotic pressure on contraction in collagen, suggesting that collagen could function as a mechanical actuator. |
doi_str_mv | 10.1038/ncomms6942 |
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Water is an important component of collagen in tendons, bone and extracellular matrix, but its role in the mechanical function of protein is poorly understood. Here, the authors study the effects of osmotic pressure on contraction in collagen, suggesting that collagen could function as a mechanical actuator.</description><identifier>ISSN: 2041-1723</identifier><identifier>EISSN: 2041-1723</identifier><identifier>DOI: 10.1038/ncomms6942</identifier><identifier>PMID: 25608644</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>119/118 ; 140/133 ; 639/301/54 ; Animals ; Bone and Bones - pathology ; Collagen - chemistry ; Female ; Humanities and Social Sciences ; Molecular Dynamics Simulation ; multidisciplinary ; Muscle Contraction ; Osmosis ; Osmotic Pressure ; Pressure ; Rats ; Rats, Sprague-Dawley ; Scattering, Radiation ; Science ; Science (multidisciplinary) ; Spectrum Analysis, Raman ; Stress, Mechanical ; Temperature ; Tendons - pathology ; Tensile Strength ; Water - chemistry ; X-Ray Diffraction ; X-Rays</subject><ispartof>Nature communications, 2015-01, Vol.6 (1), p.5942-5942, Article 5942</ispartof><rights>The Author(s) 2015</rights><rights>Copyright Nature Publishing Group Jan 2015</rights><rights>Copyright © 2015, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. 2015 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c508t-b1e658a8e24b4f1cb9ef0c77d291bf151eda9907aa5617fe81df350e6408304e3</citedby><cites>FETCH-LOGICAL-c508t-b1e658a8e24b4f1cb9ef0c77d291bf151eda9907aa5617fe81df350e6408304e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1647366636/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1647366636?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25608644$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Masic, Admir</creatorcontrib><creatorcontrib>Bertinetti, Luca</creatorcontrib><creatorcontrib>Schuetz, Roman</creatorcontrib><creatorcontrib>Chang, Shu-Wei</creatorcontrib><creatorcontrib>Metzger, Till Hartmut</creatorcontrib><creatorcontrib>Buehler, Markus J.</creatorcontrib><creatorcontrib>Fratzl, Peter</creatorcontrib><title>Osmotic pressure induced tensile forces in tendon collagen</title><title>Nature communications</title><addtitle>Nat Commun</addtitle><addtitle>Nat Commun</addtitle><description>Water is an important component of collagen in tendons, but its role for the function of this load-carrying protein structure is poorly understood. Here we use a combination of multi-scale experimentation and computation to show that water is an integral part of the collagen molecule, which changes conformation upon water removal. The consequence is a shortening of the molecule that translates into tensile stresses in the range of several to almost 100 MPa, largely surpassing those of about 0.3 MPa generated by contractile muscles. Although a complete drying of collagen would be relevant for technical applications, such as the fabrication of leather or parchment, stresses comparable to muscle contraction already occur at small osmotic pressures common in biological environments. We suggest, therefore, that water-generated tensile stresses may play a role in living collagen-based materials such as tendon or bone.
Water is an important component of collagen in tendons, bone and extracellular matrix, but its role in the mechanical function of protein is poorly understood. 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nature communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Masic, Admir</au><au>Bertinetti, Luca</au><au>Schuetz, Roman</au><au>Chang, Shu-Wei</au><au>Metzger, Till Hartmut</au><au>Buehler, Markus J.</au><au>Fratzl, Peter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Osmotic pressure induced tensile forces in tendon collagen</atitle><jtitle>Nature communications</jtitle><stitle>Nat Commun</stitle><addtitle>Nat Commun</addtitle><date>2015-01-22</date><risdate>2015</risdate><volume>6</volume><issue>1</issue><spage>5942</spage><epage>5942</epage><pages>5942-5942</pages><artnum>5942</artnum><issn>2041-1723</issn><eissn>2041-1723</eissn><abstract>Water is an important component of collagen in tendons, but its role for the function of this load-carrying protein structure is poorly understood. 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Water is an important component of collagen in tendons, bone and extracellular matrix, but its role in the mechanical function of protein is poorly understood. Here, the authors study the effects of osmotic pressure on contraction in collagen, suggesting that collagen could function as a mechanical actuator.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>25608644</pmid><doi>10.1038/ncomms6942</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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subjects | 119/118 140/133 639/301/54 Animals Bone and Bones - pathology Collagen - chemistry Female Humanities and Social Sciences Molecular Dynamics Simulation multidisciplinary Muscle Contraction Osmosis Osmotic Pressure Pressure Rats Rats, Sprague-Dawley Scattering, Radiation Science Science (multidisciplinary) Spectrum Analysis, Raman Stress, Mechanical Temperature Tendons - pathology Tensile Strength Water - chemistry X-Ray Diffraction X-Rays |
title | Osmotic pressure induced tensile forces in tendon collagen |
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