glucosepane has been researched along with arginyllysine* in 1 studies
1 other study(ies) available for glucosepane and arginyllysine
| Article | Year |
|---|---|
Effect on the mechanical properties of type I collagen of intra-molecular lysine-arginine derived advanced glycation end-product cross-linking.
Non-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. Topics: Arginine; Collagen; Collagen Type I; Connective Tissue; Cross-Linking Reagents; Dipeptides; Elasticity; Glycation End Products, Advanced; Humans; Hydrogen Bonding; Imidazoles; Lysine; Molecular Dynamics Simulation; Peptides; Protein Domains; Tensile Strength | 2018 |