A description of hydrogen bonds in the chromium(III)-crosslinked collagen: insight from the molecular dynamics simulation

The paper investigated the conformation and stability of the chromium(III)-crosslinked collagen fibers under different moisture contents by the molecular dynamics method, focusing on making a qualitative and quantitative analysis for the H-bonds. The water-mediated hydrogen bonding and direct hydrogen bonding interaction between neighboring bundles are the main driving force of the assembly of collagen fibrils. The right amount of moisture can well trig the conformation of collagen fibrils, during which water acts as a crosslinking role through the bridging hydrogen bonds. The Gly, Glu, Arg, Asp, and Lys play major roles in the formation of the direct hydrogen bonds, in which the amino acid with a long side chain, such as Arg and Glu, is particularly likely to form intrachain hydrogen bonds. The competition and disturbance of the water molecules lead to the great loss of the direct H-bonds. Anyway, a certain amount of intrachain hydrogen bonds is able to block the active sites in collagen and keep these sites away from the other molecules.