Collagen has a triple helix structure consisting of three α-polypeptide chains, with each α-peptide chain containing 600–1000 amino acids.
The amino acid composition of its unique triple helix structure provides a stabilizing effect on collagen molecules. It mainly relies on interactions between the body and cells to exhibit its specific properties and has characteristics such as biocompatibility, low immunogenicity, and biodegradability.
High tensile strength
There are three types of cross-links within collagen molecules:
- aldol condensation cross-links;
- aldolamine condensation cross-links;
- aldol histidine cross-links.
These three types of cross-links firmly connect collagen peptide chains, providing collagen with high tensile strength.