Intra-molecular lysine-arginine derived advanced glycation end-product cross-linking in Type I collagen: A molecular dynamics simulation study.

dc.citation.volume218
dc.contributor.authorCollier TA
dc.contributor.authorNash A
dc.contributor.authorBirch HL
dc.contributor.authorde Leeuw NH
dc.coverage.spatialNetherlands
dc.date.available2016-11
dc.date.available2016-09-12
dc.date.issued2016-11
dc.description.abstractCovalently cross-linked advanced glycation end products (AGE) are among the major post-translational modifications to proteins as a result of non-enzymatic glycation. The formation of AGEs has been shown to have adverse effects on the properties of the collagenous tissue; they are even linked to a number of age related disorders. Little is known about the sites at which these AGEs form or why certain sites within the collagen are energetically more favourable than others. In this study we have used a proven fully atomistic molecular dynamics approach to identify six sites where the formation of the intra-molecular 3-deoxyglucosone-derived imidazolium cross-link (DOGDIC) is energetically favourable. We have also conducted a comparison of these positions with those of the more abundant glucosepane cross-link, to determine any site preference. We show that when we consider both lysine and arginine AGEs, they exhibit a prevalence to form within the gap region of the collagen fibril.
dc.description.publication-statusPublished
dc.format.extent42 - 46
dc.identifierhttps://www.ncbi.nlm.nih.gov/pubmed/27648753
dc.identifierS0301-4622(16)30278-2
dc.identifier.citationBiophys Chem, 2016, 218 pp. 42 - 46
dc.identifier.doi10.1016/j.bpc.2016.09.003
dc.identifier.eissn1873-4200
dc.identifier.elements-id338628
dc.identifier.harvestedMassey_Dark
dc.languageeng
dc.relation.isPartOfBiophys Chem
dc.relation.urihttps://www.sciencedirect.com/science/article/pii/S0301462216302782?via=ihub
dc.rightsOpen Access funded by Biotechnology and Biological Sciences Research Council under a Creative Commons license
dc.subjectAdvanced glycation end products
dc.subjectCollagen
dc.subjectDOGDIC
dc.subjectGlucosepane
dc.subjectGlycation
dc.subjectMolecular dynamics
dc.subjectProtein cross-linking
dc.subjectAnimals
dc.subjectArginine
dc.subjectBinding Sites
dc.subjectCollagen Type I
dc.subjectCross-Linking Reagents
dc.subjectDeoxyglucose
dc.subjectGlycation End Products, Advanced
dc.subjectImidazoles
dc.subjectLysine
dc.subjectModels, Molecular
dc.subjectMolecular Dynamics Simulation
dc.subjectRats
dc.subject.anzsrc02 Physical Sciences
dc.subject.anzsrc03 Chemical Sciences
dc.subject.anzsrc06 Biological Sciences
dc.titleIntra-molecular lysine-arginine derived advanced glycation end-product cross-linking in Type I collagen: A molecular dynamics simulation study.
dc.typeJournal article
pubs.notesNot known
pubs.organisational-group/Massey University
pubs.organisational-group/Massey University/College of Sciences
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