Sequence and domain arrangements influence mechanical properties of elastin‐like polymeric elastomers
Identifieur interne : 001E45 ( Istex/Corpus ); précédent : 001E44; suivant : 001E46Sequence and domain arrangements influence mechanical properties of elastin‐like polymeric elastomers
Auteurs : Ming Miao ; Eva Sitarz ; Catherine M. Bellingham ; Emily Won ; Lisa D. Muiznieks ; Fred W. KeeleySource :
- Biopolymers [ 0006-3525 ] ; 2013-06.
Abstract
Elastin is the polymeric, extracellular matrix protein that provides properties of extensibility and elastic recoil to large arteries, lung parenchyma, and other tissues. Elastin assembles by crosslinking through lysine residues of its monomeric precursor, tropoelastin. Tropoelastin, as well as polypeptides based on tropoelastin sequences, undergo a process of self‐assembly that aligns lysine residues for crosslinking. As a result, both the full‐length monomer as well as elastin‐like polypeptides (ELPs) can be made into biomaterials whose properties resemble those of native polymeric elastin. Using both full‐length human tropoelastin (hTE) as well as ELPs, we and others have previously reported on the influence of sequence and domain arrangements on self‐assembly properties. Here we investigate the role of domain sequence and organization on the tensile mechanical properties of crosslinked biomaterials fabricated from ELP variants. In general, substitutions in ELPs involving similiar domain types (hydrophobic or crosslinking) had little effect on mechanical properties. However, modifications altering either the structure or the characteristic sequence style of these domains had significant effects on such properties. In addition, using a series of deletion and replacement constructs for full‐length hTE, we provide new insights into the role of conserved domains of tropoelastin in determining mechanical properties. © 2012 Wiley Periodicals, Inc. Biopolymers 99: 392–407, 2013.
Url:
DOI: 10.1002/bip.22192
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Elastin assembles by crosslinking through lysine residues of its monomeric precursor, tropoelastin. Tropoelastin, as well as polypeptides based on tropoelastin sequences, undergo a process of self‐assembly that aligns lysine residues for crosslinking. As a result, both the full‐length monomer as well as elastin‐like polypeptides (ELPs) can be made into biomaterials whose properties resemble those of native polymeric elastin. Using both full‐length human tropoelastin (hTE) as well as ELPs, we and others have previously reported on the influence of sequence and domain arrangements on self‐assembly properties. Here we investigate the role of domain sequence and organization on the tensile mechanical properties of crosslinked biomaterials fabricated from ELP variants. In general, substitutions in ELPs involving similiar domain types (hydrophobic or crosslinking) had little effect on mechanical properties. 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Elastin assembles by crosslinking through lysine residues of its monomeric precursor, tropoelastin. Tropoelastin, as well as polypeptides based on tropoelastin sequences, undergo a process of self‐assembly that aligns lysine residues for crosslinking. As a result, both the full‐length monomer as well as elastin‐like polypeptides (ELPs) can be made into biomaterials whose properties resemble those of native polymeric elastin. Using both full‐length human tropoelastin (hTE) as well as ELPs, we and others have previously reported on the influence of sequence and domain arrangements on self‐assembly properties. Here we investigate the role of domain sequence and organization on the tensile mechanical properties of crosslinked biomaterials fabricated from ELP variants. In general, substitutions in ELPs involving similiar domain types (hydrophobic or crosslinking) had little effect on mechanical properties. However, modifications altering either the structure or the characteristic sequence style of these domains had significant effects on such properties. In addition, using a series of deletion and replacement constructs for full‐length hTE, we provide new insights into the role of conserved domains of tropoelastin in determining mechanical properties. © 2012 Wiley Periodicals, Inc. 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However, modifications altering either the structure or the characteristic sequence style of these domains had significant effects on such properties. In addition, using a series of deletion and replacement constructs for full‐length hTE, we provide new insights into the role of conserved domains of tropoelastin in determining mechanical properties. © 2012 Wiley Periodicals, Inc. 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Elastin assembles by crosslinking through lysine residues of its monomeric precursor, tropoelastin. Tropoelastin, as well as polypeptides based on tropoelastin sequences, undergo a process of self‐assembly that aligns lysine residues for crosslinking. As a result, both the full‐length monomer as well as elastin‐like polypeptides (ELPs) can be made into biomaterials whose properties resemble those of native polymeric elastin. Using both full‐length human tropoelastin (hTE) as well as ELPs, we and others have previously reported on the influence of sequence and domain arrangements on self‐assembly properties. Here we investigate the role of domain sequence and organization on the tensile mechanical properties of crosslinked biomaterials fabricated from ELP variants. In general, substitutions in ELPs involving similiar domain types (hydrophobic or crosslinking) had little effect on mechanical properties. However, modifications altering either the structure or the characteristic sequence style of these domains had significant effects on such properties. In addition, using a series of deletion and replacement constructs for full‐length hTE, we provide new insights into the role of conserved domains of tropoelastin in determining mechanical properties. © 2012 Wiley Periodicals, Inc. Biopolymers 99: 392–407, 2013.</p></abstract></abstractGroup></contentMeta><noteGroup><note xml:id="bip22183-note-0001" numbered="no"><p>This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at <email>biopolymers@wiley.com</email></p></note></noteGroup></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Sequence and domain arrangements influence mechanical properties of elastin‐like polymeric elastomers</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Mechanical Properties of Materials from Elastin‐like Polypeptides</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Sequence and domain arrangements influence mechanical properties of elastin‐like polymeric elastomers</title></titleInfo><name type="personal"><namePart type="given">Ming</namePart><namePart type="family">Miao</namePart><affiliation>Molecular Structure and Function Program, Research Institute, The Hospital for Sick Children, 555 University Avenue, ON, M5G1X8, Toronto, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Eva</namePart><namePart type="family">Sitarz</namePart><affiliation>Molecular Structure and Function Program, Research Institute, The Hospital for Sick Children, 555 University Avenue, ON, M5G1X8, Toronto, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Catherine M.</namePart><namePart type="family">Bellingham</namePart><affiliation>Molecular Structure and Function Program, Research Institute, The Hospital for Sick Children, 555 University Avenue, ON, M5G1X8, Toronto, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Emily</namePart><namePart type="family">Won</namePart><affiliation>Molecular Structure and Function Program, Research Institute, The Hospital for Sick Children, 555 University Avenue, ON, M5G1X8, Toronto, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Lisa D.</namePart><namePart type="family">Muiznieks</namePart><affiliation>Molecular Structure and Function Program, Research Institute, The Hospital for Sick Children, 555 University Avenue, ON, M5G1X8, Toronto, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Fred W.</namePart><namePart type="family">Keeley</namePart><affiliation>Molecular Structure and Function Program, Research Institute, The Hospital for Sick Children, 555 University Avenue, M5G1X8, Toronto, ON, Canada</affiliation><affiliation>Department of Biochemistry, University of Toronto, ON M5G1X8, Canada</affiliation><affiliation>E-mail: fwk@sickkids.ca</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><dateIssued encoding="w3cdtf">2013-06</dateIssued><dateCreated encoding="w3cdtf">2013-03-21</dateCreated><dateCaptured encoding="w3cdtf">2012-08-20</dateCaptured><dateValid encoding="w3cdtf">2012-11-18</dateValid><copyrightDate encoding="w3cdtf">2013</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract>Elastin is the polymeric, extracellular matrix protein that provides properties of extensibility and elastic recoil to large arteries, lung parenchyma, and other tissues. Elastin assembles by crosslinking through lysine residues of its monomeric precursor, tropoelastin. Tropoelastin, as well as polypeptides based on tropoelastin sequences, undergo a process of self‐assembly that aligns lysine residues for crosslinking. As a result, both the full‐length monomer as well as elastin‐like polypeptides (ELPs) can be made into biomaterials whose properties resemble those of native polymeric elastin. Using both full‐length human tropoelastin (hTE) as well as ELPs, we and others have previously reported on the influence of sequence and domain arrangements on self‐assembly properties. Here we investigate the role of domain sequence and organization on the tensile mechanical properties of crosslinked biomaterials fabricated from ELP variants. In general, substitutions in ELPs involving similiar domain types (hydrophobic or crosslinking) had little effect on mechanical properties. However, modifications altering either the structure or the characteristic sequence style of these domains had significant effects on such properties. In addition, using a series of deletion and replacement constructs for full‐length hTE, we provide new insights into the role of conserved domains of tropoelastin in determining mechanical properties. © 2012 Wiley Periodicals, Inc. Biopolymers 99: 392–407, 2013.</abstract><note type="funding">Heart and Stroke Foundation of Ontario</note><subject><genre>keywords</genre><topic>elastin</topic><topic>biomaterials</topic><topic>elastin‐like polypeptides</topic><topic>sequence</topic><topic>mechanical properties</topic></subject><relatedItem type="host"><titleInfo><title>Biopolymers</title><subTitle>Original Research on Biomolecules</subTitle></titleInfo><titleInfo type="abbreviated"><title>Biopolymers</title></titleInfo><genre type="journal">journal</genre><subject><genre>article-category</genre><topic>Research Article</topic></subject><identifier type="ISSN">0006-3525</identifier><identifier type="eISSN">1097-0282</identifier><identifier type="DOI">10.1002/(ISSN)1097-0282</identifier><identifier type="PublisherID">BIP</identifier><part><date>2013</date><detail type="volume"><caption>vol.</caption><number>99</number></detail><detail type="issue"><caption>no.</caption><number>6</number></detail><extent unit="pages"><start>392</start><end>407</end><total>16</total></extent></part></relatedItem><identifier type="istex">74C4D5834655D805B0512C21609B57D69C2C9C7F</identifier><identifier type="DOI">10.1002/bip.22192</identifier><identifier type="ArticleID">BIP22192</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2012 Wiley Periodicals, Inc.Copyright © 2012 Wiley Periodicals, Inc.</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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