Effect on the mechanical properties of type I collagen of intra-molecular lysine-arginine derived advanced glycation end-product cross-linking

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dc.citation.volume67
dc.contributor.authorCollier TA
dc.contributor.authorNash A
dc.contributor.authorBirch HL
dc.contributor.authorde Leeuw NH
dc.date.available2018-01-23
dc.date.available2017-11-22
dc.date.issued2017-11-28
dc.description.abstractNon-enzymatic advanced glycation end product (AGE) cross-linking of collagen molecules has been hypothesised to result in significant changes to the mechanical properties of the connective tissues within the body, potentially resulting in a number of age related diseases. We have investigated the effect of two of these cross-links, glucosepane and DOGDIC, on the tensile and lateral moduli of the collagen molecule through the use of a steered molecular dynamics approach, using previously identified preferential formation sites for intra-molecular cross-links. Our results show that the presence of intra-molecular AGE cross-links increases the tensile and lateral Young’s moduli in the low strain domain by between 3.0 - 8.5 % and 2.9 - 60.3 % respectively, with little effect exhibited at higher strains.
dc.description.publication-statusPublished
dc.format.extent55 - 61
dc.identifierhttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000424172300008&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=c5bb3b2499afac691c2e3c1a83ef6fef
dc.identifier.citationJOURNAL OF BIOMECHANICS, 2018, 67 pp. 55 - 61
dc.identifier.doi10.1016/j.jbiomech.2017.11.021
dc.identifier.eissn1873-2380
dc.identifier.elements-id396935
dc.identifier.harvestedMassey_Dark
dc.identifier.issn0021-9290
dc.publisherElsevier
dc.relation.isPartOfJOURNAL OF BIOMECHANICS
dc.relation.replaceshttp://hdl.handle.net/123456789/11742
dc.relation.replaces123456789/11742
dc.relation.urihttp://www.jbiomech.com/article/S0021-9290(17)30672-3/fulltext
dc.rightsOpen Access funded by Biotechnology and Biological Sciences Research Council nder a Creative Commons license
dc.subjectCollagen
dc.subjectMolecular dynamics
dc.subjectAgeing
dc.subjectGlycation
dc.subjectProtein cross-linking
dc.subjectMolecular biomechanics
dc.subject.anzsrc0903 Biomedical Engineering
dc.subject.anzsrc0913 Mechanical Engineering
dc.subject.anzsrc1106 Human Movement and Sports Sciences
dc.titleEffect on the mechanical properties of type I collagen of intra-molecular lysine-arginine derived advanced glycation end-product cross-linking
dc.typeJournal article
pubs.notesNot known
pubs.organisational-group/Massey University
pubs.organisational-group/Massey University/College of Sciences
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