Abstract
Collagen Type I derived from fish is mainly limited by its poor physicochemical properties for further applications. In this study, we developed epigallocatechin gallate (EGCG) cross-linked collagen hydrogels (EC hydrogels) to realize physicochemical improvements, basing on the interaction mechanism between collagen and EGCG. The integrity of collagen framework with slight secondary structure change in the presence of EGCG was confirmed. The stronger stability of collagen fibrils was proved by slower swelling ratio, declined enzymatic degradation, improved thermal analysis and mechanical test due to EGCG modification. To illustrate the potential mechanism between collagen and EGCG, molecular docking was used to identify both covalent (CN bond, between lysine of collagen and C2-ring B of EGCG) and non-covalent bonds (hydrogen bond and hydrophobic interaction) within in EC hydrogel. Taken together, this work would offer some insights into the further study about the interaction between EGCG and collagen.
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