Collier TANash ABirch HLde Leeuw NH2016-112016-09-122016-11Biophys Chem, 2016, 218 pp. 42 - 46https://hdl.handle.net/10179/13043Covalently 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.42 - 46Advanced glycation end productsCollagenDOGDICGlucosepaneGlycationMolecular dynamicsProtein cross-linkingAnimalsArginineBinding SitesCollagen Type ICross-Linking ReagentsDeoxyglucoseGlycation End Products, AdvancedImidazolesLysineModels, MolecularMolecular Dynamics SimulationRatsJournal article10.1016/j.bpc.2016.09.0033386281873-4200Massey_Dark02 Physical Sciences03 Chemical Sciences06 Biological Sciences