Abstract
Collagen, the most abundant protein in mammalian tissues, has been widely used in biomedical materials. Many researchers have been performing various modifications on collagen to increase its applicability. Different non-covalent interactions were also applied to promote the self-assembly of collagen into higher order structure. Collagen is a right-handed triple helix, and each helix is a left-handed polyproline type II structure containing many (X-Y-Gly)n repeats. On the other hand, carbohydrates are a necessity to organism and play an important role in biological functions. In this work, we modified (2S,4R)-hydroxyproline with 1.2,3,4,6-penta-O-acetyl-β-D-galactopyranoside and synthesized a series of collagen-related peptides containing this modified amino acid to study the consequences of glycosylation on collagen stability and self-assembly. CD measurements indicate that glycosylation will destabilize the collagen triple helices. However, TEM shows that the modification promotes the self-assembly of collagen-related peptides into higher-order structures, suggesting that glycosylation could enhance the interactions between collagen-related peptides to speed their assembly.