Stabilization and anomalous hydration of collagen fibril under heating
Type I collagen is the most common protein among higher vertebrates. It forms the basis of fibrous connective tissues (tendon, chord, skin, bones) and ensures mechanical stability and strength of these tissues. It is known, however, that separate triple-helical collagen macromolecules are unstable a...
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| Veröffentlicht in: | PloS one 2013-11, Vol.8 (11), p.e78526-e78526 |
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| creator | Gevorkian, Sasun G Allahverdyan, Armen E Gevorgyan, David S Simonian, Aleksandr L Hu, Chin-Kun |
| description | Type I collagen is the most common protein among higher vertebrates. It forms the basis of fibrous connective tissues (tendon, chord, skin, bones) and ensures mechanical stability and strength of these tissues. It is known, however, that separate triple-helical collagen macromolecules are unstable at physiological temperatures. We want to understand the mechanism of collagen stability at the intermolecular level. To this end, we study the collagen fibril, an intermediate level in the collagen hierarchy between triple-helical macromolecule and tendon.
When heating a native fibril sample, its Young's modulus decreases in temperature range 20-58°C due to partial denaturation of triple-helices, but it is approximately constant at 58-75°C, because of stabilization by inter-molecular interactions. The stabilization temperature range 58-75°C has two further important features: here the fibril absorbs water under heating and the internal friction displays a peak. We relate these experimental findings to restructuring of collagen triple-helices in fibril. A theoretical description of the experimental results is provided via a generalization of the standard Zimm-Bragg model for the helix-coil transition. It takes into account intermolecular interactions of collagen triple-helices in fibril and describes water adsorption via the Langmuir mechanism.
We uncovered an inter-molecular mechanism that stabilizes the fibril made of unstable collagen macromolecules. This mechanism can be relevant for explaining stability of collagen. |
| doi_str_mv | 10.1371/journal.pone.0078526 |
| format | Article |
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When heating a native fibril sample, its Young's modulus decreases in temperature range 20-58°C due to partial denaturation of triple-helices, but it is approximately constant at 58-75°C, because of stabilization by inter-molecular interactions. The stabilization temperature range 58-75°C has two further important features: here the fibril absorbs water under heating and the internal friction displays a peak. We relate these experimental findings to restructuring of collagen triple-helices in fibril. A theoretical description of the experimental results is provided via a generalization of the standard Zimm-Bragg model for the helix-coil transition. It takes into account intermolecular interactions of collagen triple-helices in fibril and describes water adsorption via the Langmuir mechanism.
We uncovered an inter-molecular mechanism that stabilizes the fibril made of unstable collagen macromolecules. This mechanism can be relevant for explaining stability of collagen.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0078526</identifier><identifier>PMID: 24244320</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Analysis ; Animals ; Bones ; Collagen ; Collagen (type I) ; Collagen - chemistry ; Connective tissues ; Denaturation ; Heat ; Heating ; Helices ; Hot Temperature ; Hydration ; Internal friction ; Macromolecules ; Mechanical properties ; Modulus of elasticity ; Molecular interactions ; Phase transitions ; Physics ; Physiological aspects ; Physiology ; Polymers ; Polypeptides ; Protein denaturation ; Protein Stability ; Protein Structure, Secondary ; Proteins ; Rats ; Skin ; Stability ; Stabilization ; Temperature ; Temperature range ; Theory ; Tissues ; Vertebrates ; Viscoelasticity</subject><ispartof>PloS one, 2013-11, Vol.8 (11), p.e78526-e78526</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013 Gevorkian et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2013 Gevorkian et al 2013 Gevorkian et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c758t-4889cfef7d2e0db87171beb967cbce11625942673c15e6cf4277b8188b49dc4b3</citedby><cites>FETCH-LOGICAL-c758t-4889cfef7d2e0db87171beb967cbce11625942673c15e6cf4277b8188b49dc4b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3823754/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3823754/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79569,79570</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24244320$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gevorkian, Sasun G</creatorcontrib><creatorcontrib>Allahverdyan, Armen E</creatorcontrib><creatorcontrib>Gevorgyan, David S</creatorcontrib><creatorcontrib>Simonian, Aleksandr L</creatorcontrib><creatorcontrib>Hu, Chin-Kun</creatorcontrib><title>Stabilization and anomalous hydration of collagen fibril under heating</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Type I collagen is the most common protein among higher vertebrates. It forms the basis of fibrous connective tissues (tendon, chord, skin, bones) and ensures mechanical stability and strength of these tissues. It is known, however, that separate triple-helical collagen macromolecules are unstable at physiological temperatures. We want to understand the mechanism of collagen stability at the intermolecular level. To this end, we study the collagen fibril, an intermediate level in the collagen hierarchy between triple-helical macromolecule and tendon.
When heating a native fibril sample, its Young's modulus decreases in temperature range 20-58°C due to partial denaturation of triple-helices, but it is approximately constant at 58-75°C, because of stabilization by inter-molecular interactions. The stabilization temperature range 58-75°C has two further important features: here the fibril absorbs water under heating and the internal friction displays a peak. We relate these experimental findings to restructuring of collagen triple-helices in fibril. A theoretical description of the experimental results is provided via a generalization of the standard Zimm-Bragg model for the helix-coil transition. It takes into account intermolecular interactions of collagen triple-helices in fibril and describes water adsorption via the Langmuir mechanism.
We uncovered an inter-molecular mechanism that stabilizes the fibril made of unstable collagen macromolecules. 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gevorkian, Sasun G</au><au>Allahverdyan, Armen E</au><au>Gevorgyan, David S</au><au>Simonian, Aleksandr L</au><au>Hu, Chin-Kun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Stabilization and anomalous hydration of collagen fibril under heating</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2013-11-11</date><risdate>2013</risdate><volume>8</volume><issue>11</issue><spage>e78526</spage><epage>e78526</epage><pages>e78526-e78526</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Type I collagen is the most common protein among higher vertebrates. It forms the basis of fibrous connective tissues (tendon, chord, skin, bones) and ensures mechanical stability and strength of these tissues. It is known, however, that separate triple-helical collagen macromolecules are unstable at physiological temperatures. We want to understand the mechanism of collagen stability at the intermolecular level. To this end, we study the collagen fibril, an intermediate level in the collagen hierarchy between triple-helical macromolecule and tendon.
When heating a native fibril sample, its Young's modulus decreases in temperature range 20-58°C due to partial denaturation of triple-helices, but it is approximately constant at 58-75°C, because of stabilization by inter-molecular interactions. The stabilization temperature range 58-75°C has two further important features: here the fibril absorbs water under heating and the internal friction displays a peak. We relate these experimental findings to restructuring of collagen triple-helices in fibril. A theoretical description of the experimental results is provided via a generalization of the standard Zimm-Bragg model for the helix-coil transition. It takes into account intermolecular interactions of collagen triple-helices in fibril and describes water adsorption via the Langmuir mechanism.
We uncovered an inter-molecular mechanism that stabilizes the fibril made of unstable collagen macromolecules. This mechanism can be relevant for explaining stability of collagen.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24244320</pmid><doi>10.1371/journal.pone.0078526</doi><tpages>e78526</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Analysis Animals Bones Collagen Collagen (type I) Collagen - chemistry Connective tissues Denaturation Heat Heating Helices Hot Temperature Hydration Internal friction Macromolecules Mechanical properties Modulus of elasticity Molecular interactions Phase transitions Physics Physiological aspects Physiology Polymers Polypeptides Protein denaturation Protein Stability Protein Structure, Secondary Proteins Rats Skin Stability Stabilization Temperature Temperature range Theory Tissues Vertebrates Viscoelasticity |
| title | Stabilization and anomalous hydration of collagen fibril under heating |
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