Computational Simulation and Analysis of the Transverse Isotropic Property of Glycosaminoglycan in Collagen
Year: 2025
Type: conference-paper
Abstract: Glycosaminoglycans (GAGs) are disaccharides chains that are linked to a polypeptide core that serves as a crosslink in collagen to provide strength and persistency for collagen and related tissue.GAGs serve in two roles in Collagen-GAGs matrix.One is to connect collagen fibers in the matrix, and the other one is to contribute in the mechanical properties of the matrix.This paper summarizes the study of the isotropy of GAGs distribution in transverse plane of aligned collagen fibrils based on the roles of GAGs.The angle of GAGs related to collagen fibrils were used as parameter to qualify the GAGs isotropic characteristic in both 3D and 2D rendering.Statistical results included that over one third percentage of GAGs were closed to perpendicular direction to collagen fibril with symmetrical distribution for both 3D matrix and 2D plane cross through collagen fibrils.The three factors tested in this paper: collagen radius, collagen distribution, and GAGs density, were not statistically significant for the strength of Collagen-GAG matrix in 3D rendering.However in 2D rendering, a significant factor found was the radius of collagen in matrix for the GAGs directed to orthogonal plane of Collagen-GAG matrix.Between two cross-section selected from Collagen-GAG matrix model, the plane cross through collagen fibrils was symmetrically distributed but the peak located at orthogonal plan was deducted by decreasing collagen radius.There were some symmetry features of GAGs angle distribution in selected 2D plane passed through space between collagen fibrils, but most models showed multiple peaks in GAGs angle distribution.With less GAGs directed to perpendicular of collagen fibril, strength in collagen cross-section weakened.Collagen distribution was also a factor that influence GAGs angle distribution in 2D rendering.True hexagonal collagen packaging was reported in this paper to be less strength at collagen cross-section compared with quasihexagonal collagen arrangement.
Authors: Bi Yuying, Prabir Patra
Language: English
Subfield: Biomedical Engineering
Field: Engineering
Domain: Physical Sciences
Open Access status: gold
OpenAlex ID: W4409108966