Vitexin Inhibits Protein Glycation through Structural Protection, Methylglyoxal Trapping, and Alteration of Glycation Site

In this study, the antiglycation potential and mechanisms of vitexin were explored in vitro by multispectroscopy, microscope imaging, high-resolution mass spectrometry, and computational simulations. Vitexin was found to show much stronger antiglycation effects than aminoguanidine. The inhibition against the fluorescent advanced glycation end products was more than 80% at 500 mu M vitexin in both bovine serum albumin (BSA)-fructose and BSA-methylglyoxal (MGO) models. Treated with 100 and 200 mu M vitexin for 24 h, the contents of MGO were reduced to 4.97 and 0.2%, respectively, and only one vitexin-mono-MGO adduct was formed. LC-Orbitrap-MS/MS analysis showed that vitexin altered the glycated sites and reduced the glycation degree of some sites. The mechanisms of vitexin against protein glycation were mainly through BSA structural protection, MGO trapping, and alteration of glycation sites induced by interaction with BSA. These findings provided valuable information about the functional development of vitexin as a potential antiglycation agent.

Automated summary

Vitexin was found to exhibit strong antiglycation effects by protecting protein structure, trapping MGO, and altering glycation sites, thereby reducing the glycation degree and forming only one vitexin-mono-MGO adduct. This study provides valuable information for the development of vitexin as a potential antiglycation agent.