Inhibitory mechanism of catechins against advanced glycation end products of glycated myofibrillar protein through anti-aggregation and anti-oxidation

Protein aggregation and oxidation could induce the generation of advanced glycation end products (AGEs). N epsilon carboxymethyl lysine (CML), N epsilon-carboxyethyllysine (CEL) are two typical AGEs markers in muscle foods. Catechins are considered to be excellent natural antioxidants for scavenging AGEs in muscle protein. We compared, for the first time, the inhibitory effects and explored mechanisms of (-)-epigallocatechin (EGC), (-)-epigallocatechin-3-gallate (EGCG), (-)-epicatechin (EC), and (-)-epicatechin-3-gallate (ECG), in glycated myofibrillar protein (MPG) by measuring AGEs level, Maillard reaction degree, particle size and anti-oxidation ability using microstructure, multispectral and molecular docking techniques. The results showed that catechins dosedependently inhibited AGEs in MPG through influencing lysine and free amino group, alleviating the Maillard reaction, detaching the particle size, affecting the protein-catechins interaction, relieving aggregates, and scavenging free radicals. The underlying mechanism behind the result indicated that catechins altered the structure information, SDS-PAGE bands, and the interaction sites of MPG via anti-aggregation and anti-oxidation. Particularly, EC and ECG showed weaker antioxidant ability than EGC and EGCG, EGCG exhibited a significant Pearson's correlation with the anti-oxidation and anti-aggregation of CML but no significant association with CEL. Overall, this study provides a theoretical insight into the applications of catechins to muscle foods as AGEs inhibitors.

Automated summary

The study demonstrates that catechins can inhibit the generation of AGEs in muscle protein through various mechanisms, including influencing lysine and free amino group, alleviating the Maillard reaction, detaching the particle size, affecting the protein-catechins interaction, relieving aggregates, and scavenging free radicals.