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Lysine-Arginine Advanced Glycation End-Product Cross-links and the Effect on Collagen Structure: A Molecular Dynamics Study

Nash, A; Noh, SY; Birch, HL; de Leeuw, NH; (2020) Lysine-Arginine Advanced Glycation End-Product Cross-links and the Effect on Collagen Structure: A Molecular Dynamics Study. Proteins 10.1002/prot.26036. (In press). Green open access

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Abstract

The accumulation of advanced glycation end-products is a fundamental process that is central to age-related decline in musculoskeletal tissues and locomotor system function and other collagen-rich tissues. However, although computational studies of advanced glycation end-product cross-links could be immensely valuable, this area remains largely unexplored given the limited availability of structural parameters for the derivation of force fields for Molecular Dynamics simulations. In this article, we present the bonded force constants, atomic partial charges and geometry of the arginine-lysine cross-links DOGDIC, GODIC, and MODIC. We have performed in vacuo Molecular Dynamics simulations to validate their implementation against quantum mechanical frequency calculations. A DOGDIC advanced glycation endproduct cross-link was then inserted into a model collagen fibril to explore structural changes of collagen and dynamics in interstitial water. Unlike our previous studies of glucosepane, our findings suggest that intra-collagen DOGDIC cross-links furthers intra-collagen peptide hydrogen-bonding and does not promote the diffusion of water through the collagen triple helices.

Type: Article
Title: Lysine-Arginine Advanced Glycation End-Product Cross-links and the Effect on Collagen Structure: A Molecular Dynamics Study
Location: United States
Open access status: An open access version is available from UCL Discovery
DOI: 10.1002/prot.26036
Publisher version: https://doi.org/10.1002/prot.26036
Language: English
Additional information: This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. http://creativecommons.org/licenses/by/4.0/
Keywords: advanced glycation end-products, aging, collagen, cross-linking, DOGDIC, glucosepane, matrix biology
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Div of Surgery and Interventional Sci
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Div of Surgery and Interventional Sci > Department of Ortho and MSK Science
URI: https://discovery.ucl.ac.uk/id/eprint/10118421
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