Facile Control over the Supramolecular Ordering of Self-assembled Peptide Scaffolds by Simultaneous Assembly with a Polysacharride.
Identifieur interne : 000C44 ( PubMed/Checkpoint ); précédent : 000C43; suivant : 000C45Facile Control over the Supramolecular Ordering of Self-assembled Peptide Scaffolds by Simultaneous Assembly with a Polysacharride.
Auteurs : Rui Li [Australie] ; Mitchell Boyd-Moss [Australie] ; Benjamin Long [Australie] ; Anne Martel [France] ; Andrew Parnell [Royaume-Uni] ; Andrew J C. Dennison [Royaume-Uni] ; Colin J. Barrow [Australie] ; David R. Nisbet [Australie] ; Richard J. Williams [Australie]Source :
- Scientific reports [ 2045-2322 ] ; 2017.
Abstract
Enabling control over macromolecular ordering and the spatial distribution of structures formed via the mechanisms of molecular self-assembly is a challenge that could yield a range of new functional materials. In particular, using the self-assembly of minimalist peptides, to drive the incorporation of large complex molecules will allow a functionalization strategy for the next generation of biomaterial engineering. Here, for the first time, we show that co-assembly with increasing concentrations of a highly charged polysaccharide, fucoidan, the microscale ordering of Fmoc-FRGDF peptide fibrils and subsequent mechanical properties of the resultant hydrogel can be easily and effectively manipulated without disruption to the nanofibrillar structure of the assembly.
DOI: 10.1038/s41598-017-04643-3
PubMed: 28684767
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Dennison</name><affiliation wicri:level="1"><nlm:affiliation>Department of Physics and Astronomy, University of Sheffield, Sheffield, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Physics and Astronomy, University of Sheffield, Sheffield</wicri:regionArea><wicri:noRegion>Sheffield</wicri:noRegion></affiliation></author><author><name sortKey="Barrow, Colin J" sort="Barrow, Colin J" uniqKey="Barrow C" first="Colin J" last="Barrow">Colin J. 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David.Nisbet@ANU.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Laboratory of Advanced Biomaterials, Research School of Engineering, The Australian National University, Canberra, ACT</wicri:regionArea><wicri:noRegion>ACT</wicri:noRegion></affiliation></author><author><name sortKey="Williams, Richard J" sort="Williams, Richard J" uniqKey="Williams R" first="Richard J" last="Williams">Richard J. Williams</name><affiliation wicri:level="1"><nlm:affiliation>School of Engineering, RMIT University, Melbourne, Victoria, Australia. Richard.Williams@RMIT.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Engineering, RMIT University, Melbourne, Victoria</wicri:regionArea><wicri:noRegion>Victoria</wicri:noRegion></affiliation></author></analytic><series><title level="j">Scientific reports</title><idno type="eISSN">2045-2322</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Enabling control over macromolecular ordering and the spatial distribution of structures formed via the mechanisms of molecular self-assembly is a challenge that could yield a range of new functional materials. In particular, using the self-assembly of minimalist peptides, to drive the incorporation of large complex molecules will allow a functionalization strategy for the next generation of biomaterial engineering. Here, for the first time, we show that co-assembly with increasing concentrations of a highly charged polysaccharide, fucoidan, the microscale ordering of Fmoc-FRGDF peptide fibrils and subsequent mechanical properties of the resultant hydrogel can be easily and effectively manipulated without disruption to the nanofibrillar structure of the assembly.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">28684767</PMID><DateCreated><Year>2017</Year><Month>07</Month><Day>07</Day></DateCreated><DateRevised><Year>2017</Year><Month>07</Month><Day>14</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2045-2322</ISSN><JournalIssue CitedMedium="Internet"><Volume>7</Volume><Issue>1</Issue><PubDate><Year>2017</Year><Month>Jul</Month><Day>06</Day></PubDate></JournalIssue><Title>Scientific reports</Title><ISOAbbreviation>Sci Rep</ISOAbbreviation></Journal><ArticleTitle>Facile Control over the Supramolecular Ordering of Self-assembled Peptide Scaffolds by Simultaneous Assembly with a Polysacharride.</ArticleTitle><Pagination><MedlinePgn>4797</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/s41598-017-04643-3</ELocationID><Abstract><AbstractText>Enabling control over macromolecular ordering and the spatial distribution of structures formed via the mechanisms of molecular self-assembly is a challenge that could yield a range of new functional materials. In particular, using the self-assembly of minimalist peptides, to drive the incorporation of large complex molecules will allow a functionalization strategy for the next generation of biomaterial engineering. Here, for the first time, we show that co-assembly with increasing concentrations of a highly charged polysaccharide, fucoidan, the microscale ordering of Fmoc-FRGDF peptide fibrils and subsequent mechanical properties of the resultant hydrogel can be easily and effectively manipulated without disruption to the nanofibrillar structure of the assembly.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Rui</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Center for Chemistry and Biotechnology, Deakin University, Waurn Ponds, VIC, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Boyd-Moss</LastName><ForeName>Mitchell</ForeName><Initials>M</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-8670-8477</Identifier><AffiliationInfo><Affiliation>School of Engineering, RMIT University, Melbourne, Victoria, Australia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Biofab3D, St. Vincents Hospital, Melbourne, Victoria, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Long</LastName><ForeName>Benjamin</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Center for Chemistry and Biotechnology, Deakin University, Waurn Ponds, VIC, Australia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>School of Applied and Biomedical Sciences, Federation University, Mount Helen, Victoria, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Martel</LastName><ForeName>Anne</ForeName><Initials>A</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-1232-8519</Identifier><AffiliationInfo><Affiliation>Institut Laue Langevin, Grenoble, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Parnell</LastName><ForeName>Andrew</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Physics and Astronomy, University of Sheffield, Sheffield, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dennison</LastName><ForeName>Andrew J C</ForeName><Initials>AJC</Initials><AffiliationInfo><Affiliation>Department of Physics and Astronomy, University of Sheffield, Sheffield, United Kingdom.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Institut Laue Langevin, Grenoble, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry, Technical University Berlin, 10623, Berlin, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Barrow</LastName><ForeName>Colin J</ForeName><Initials>CJ</Initials><AffiliationInfo><Affiliation>Center for Chemistry and Biotechnology, Deakin University, Waurn Ponds, VIC, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nisbet</LastName><ForeName>David R</ForeName><Initials>DR</Initials><AffiliationInfo><Affiliation>Laboratory of Advanced Biomaterials, Research School of Engineering, The Australian National University, Canberra, ACT, Australia. David.Nisbet@ANU.edu.au.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Williams</LastName><ForeName>Richard J</ForeName><Initials>RJ</Initials><Identifier Source="ORCID">http://orcid.org/0000-0001-7627-7522</Identifier><AffiliationInfo><Affiliation>School of Engineering, RMIT University, Melbourne, Victoria, Australia. Richard.Williams@RMIT.edu.au.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Biofab3D, St. Vincents Hospital, Melbourne, Victoria, Australia. Richard.Williams@RMIT.edu.au.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>07</Month><Day>06</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Sci Rep</MedlineTA><NlmUniqueID>101563288</NlmUniqueID><ISSNLinking>2045-2322</ISSNLinking></MedlineJournalInfo><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Science. 2012 Feb 17;335(6070):813-7</RefSource><PMID Version="1">22344437</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Chem Soc Rev. 2008 Apr;37(4):664-75</RefSource><PMID Version="1">18362975</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Acta Biomater. 2014 Apr;10(4):1671-82</RefSource><PMID Version="1">23958781</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Biomaterials. 2011 Aug;32(22):5304-10</RefSource><PMID Version="1">21531457</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Ann Hematol. 2011 Sep;90(9):1005-15</RefSource><PMID Version="1">21327939</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Science. 2002 Mar 29;295(5564):2418-21</RefSource><PMID Version="1">11923529</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Wiley Interdiscip Rev Nanomed Nanobiotechnol. 2013 Nov-Dec;5(6):582-612</RefSource><PMID Version="1">23929805</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Nat Biotechnol. 2003 Oct;21(10):1171-8</RefSource><PMID Version="1">14520402</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Nat Nanotechnol. 2009 Jan;4(1):19-24</RefSource><PMID Version="1">19119277</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biomed Mater Res A. 2008 Jun 1;85(3):619-27</RefSource><PMID Version="1">17806115</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Faraday Discuss. 2009;143:293-303; 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