In this study, four Monascus pigments (ankaflavin, AK; monascin MS; rubropunctatin, O1; monascorubrin, O2) were proved to exhibit considerable anti-glycation properties in bovine serum albumin (BSA)-fructose model. AK (40.62 %) and MS (48.38 %) were found to exert lower inhibitory effects on the formation of fluorescent advanced glycation end products (AGEs) than aminoguanidine (59.4 %), while O1 (90.64 %) and O2 (93.82 %) displayed much stronger abilities. AK and MS could trap methylglyoxal (MGO) with maximum capture rates of 85.67 % and 84.90 %, respectively, and only mono-MGO adducts of them were detected. LC-Orbitrap MS/MS analysis revealed that four pigments significantly altered the type and reduced the number of the glycated sites and they all covalently bound to BSA, with O1 and O2 possessing high reactivity. Altogether, AK and MS suppressed fluorescent AGEs formation mainly via trapping MGO and covalently interacting with BSA, and blocking free amino groups was the dominant mechanism for O1 and O2. These findings presented new insights into Monascus pigments as dietary supplement for inhibiting protein glycation.