title: Molecular simulations predict novel collagen conformations during cross-link loading.
abstract: Collagen cross-linking mechanically strengthens tissues during development and aging, but there is limited data describing how force transmitted across cross-links affects molecular conformation. We used Steered Molecular Dynamics (SMD) to model perpendicular force through a side chain. Results predicted that collagen peptides have negligible bending resistance and that mechanical force causes helix disruption below covalent bond failure strength, suggesting alternative molecular conformations precede cross-link rupture and macroscopic damage during mechanical loading.
authors.affiliation: Physiology, Biophysics & Systems Biology Program, Weill Graduate School of Medical Sciences, Cornell University, 1300 York Avenue, New York, NY 10065, USA. BourneJ@HSS.EDU
authors.forename: Jonathan W
authors.initials: JW
authors.lastname: Bourne
authors.forename: Peter A
authors.initials: PA
authors.lastname: Torzilli
mesh_terms: D001120:Arginine / Q000737:chemistry; D003094:Collagen / Q000737:chemistry*; D003432:Cross-Linking Reagents / Q000737:chemistry*; D004548:Elasticity; D055595:Mechanical Phenomena; D008956:Models, Chemical; D056004:Molecular Dynamics Simulation; D010455:Peptides / Q000737:chemistry*; D011392:Proline / Q000737:chemistry; D011487:Protein Conformation; D013718:Tensile Strength
chemical_list: D003432:Cross-Linking Reagents; D010455:Peptides; D003094:Collagen; D001120:Arginine; D011392:Proline