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

Collier, T A; Nash, A; Birch, H L; de Leeuw, N H

Collier, T A; Nash, A; Birch, H L; de Leeuw, N H.

Affiliation

Collier TA; Institute of Natural and Mathematical Sciences, Massey University, Auckland 0632, New Zealand.
Nash A; Department of Physiology, Anatomy and Genetics, University of Oxford, South Parks Road, Oxford OX1 3QX, United Kingdom.
Birch HL; Institute of Orthopaedics and Musculoskeletal Science, UCL, RNOH Stanmore Campus, London, United Kingdom.
de Leeuw NH; School of Chemistry, Cardiff University, Cardiff CF10 1DF, United Kingdom. Electronic address: DeLeeuwN@cardiff.ac.uk.

J Biomech ; 67: 55-61, 2018 01 23.

Article in En | MEDLINE | ID: mdl-29254633

Subject(s)

Collagen Type I/chemistry; Cross-Linking Reagents/chemistry; Glycation End Products, Advanced/chemistry; Arginine/chemistry; Collagen/chemistry; Connective Tissue/physiology; Dipeptides; Elasticity; Humans; Hydrogen Bonding; Imidazoles/chemistry; Lysine/analogs & derivatives; Lysine/chemistry; Molecular Dynamics Simulation; Peptides/chemistry; Protein Domains; Tensile Strength

Key words

Ageing; Collagen; Glycation; Molecular biomechanics; Molecular dynamics; Protein cross-linking

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Glycation End Products, Advanced / Cross-Linking Reagents / Collagen Type I Limits: Humans Language: En Journal: J Biomech Year: 2018 Document type: Article

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