Collagen peptide simulated bending after applied axial deformation.

In this study we used steered molecular dynamics to first model a collagen peptide under axial tension and then apply a perpendicular bending force. Axial tension causes molecular elongation and increased the subsequent perpendicular bending stiffness, but surprisingly did not increase the predicted collagen triple helix microunfolding threshold. We believe these results elucidate a key potential mechanism by which microscale mechanical loads translate from cellular and micro scales down to the nano and atomistic. Further, these data predict that cryptic force-induced collagen triple helix unwinding is axial-deformation independent, supporting the possibility that cell traction forces could be a key molecular mechanism to alter the cellular matrix microenvironment to facilitate collagen enzymatic degradation and subsequent cellular migration, such as in tumor extravasation. PMID: 32469728 [PubMed - as supplied by publisher]
Source: Journal of the Mechanical Behavior of Biomedical Materials - Category: Materials Science Authors: Tags: J Mech Behav Biomed Mater Source Type: research