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Non-enzymatic glycosylation of proteins results in the formation of advanced glycation end products (AGEs). AGE modification of proteins and thereby damages to cells and tissues have been confirmed to contribute to the pathophysiology of aging and long-term complications of various age-related diseases. Anti-AGEs therapy has thus received significant attention, and several flavonoids including quercetin (1) and (−)-epigallocatechin gallate (EGCG) (2) have shown anti-AGEs activity through trapping and inactivating methylglyoxal (MGO), the crucial intermediate of AGEs formation. However, in the field of MGO-scavenging activity, (−)-epigallocatechin (EGC) (3), one of the key flavonoids in green tea, has received less attention compared with other flavonoids. In this study, we have shown strong MGO-scavenging activity of EGC (3), and EGC (3) was found to be equipotent to previously identified MGO-scavengers such as quercetin (1) and EGCG (2).

applied biological chemistry

Identification of (−)-epigallocatechin (EGC) as a methylglyoxal (MGO)-trapping agent and thereby as an inhibitor of advanced glycation end product (AGE) formation