Protein glycosylation inhibitory effects and mechanisms of phloretin and phlorizin

The anti-glycation potential and mechanism of phloretin and phlorizin were investigated in the study. In the methylglyoxal (MGO)-human serum albumin (HSA) glycosylation system, the inhibition against fluorescent advanced glycosylation end products (AGEs) was more than 60% at 960 μM phloretin and phlorizin. They decreased carbonylation and oxidative damage of protein, protected thiol groups and secondary structure of protein and inhibited protein aggregates. Treated with 1.37 mM phloretin or phlorizin, O 2 − · scavenging was more than 80%, and 1 mM phloretin or phlorizin chelated 60.08% or 28.11% of Fe 2+ , respectively. Analysis of HPLC and LC-QqQ-MS shown phloretin captured MGO by forming adducts with MGO, with capture rates of 92.67% within 24 h. The capture rate of phlorizin to MGO was 56.40%. The anti-glycosylation mechanisms of them could include the structural protection of HSA, capture of MGO, O 2 − · and ·OH scavenging and chelation of Fe 2+ . These findings may provide a theoretical basis for the application of phloretin and phlorizin as novel anti-glycosylation agents.