Food and Fermentation Industries >

2026 , Vol. 52 >Issue 12: 161 - 167

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.044397

Inhibitory effect of hydroxysafflor yellow A on formation of advanced glycation end products

  • WANG Jiamin ,
  • ZHANG Bohui ,
  • WANG Laizhong ,
  • GUO Limin ,
  • BAO Xiaowei
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  • 1(School of Food Science and Pharmacy, Xinjiang Agricultural University, Urumqi 830052, China)
    2(Institute of Agro-Products Storage and Processing, Xinjiang Academy of Agricultural Sciences, Urumqi 830091, China)
    3(Xinjiang Hongzhan Characteristic Agricultural Technology Development Co.Ltd., Tacheng 834800, China)

Received date: 2025-09-03

  Revised date: 2025-10-30

  Online published: 2026-07-17

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Abstract

This study aimed to explore the effect of hydroxysafflor yellow A (HSYA) on the formation of advanced glycation end products (AGEs).By establishing a simulated glycation system using bovine serum protein (BSA) and methylglyoxal (MGO), combined with spectroscopic analysis, molecular docking, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), this study quantitatively measured fluorescent AGEs, protein oxidation products (dityrosine, kynurenine, N-formylkynurenine) in the system to investigate the binding characteristics of HSYA with BSA.Results showed that HSYA at 300 μmol/L achieved inhibition rates of 70.07%, 51.71%, 68.34% and 80.37% on fluorescent AGEs, dityrosine, kynurenine and N-formylkynurenine, respectively.Fluorescence spectroscopy results showed that the existence of a binding site between HSYA and BSA.The quenching mechanism was static quenching and the main forces were hydrogen bonds and van der Waals forces.SDS-PAGE results showed that HSYA could inhibit the formation of BSA cross-linked structures in the BSA-MGO system.Molecular docking results showed that HSYA can bind to the TRP-213 residue of BSA to form a complex with BSA, and at the same time there is a hydrogen bond and van der Waals force between the ARG residue of BSA, which hinders the binding of BSA glycosylation sites to MGO, thereby inhibiting the production of AGEs.Therefore, HSYA has the potential to be developed as a natural inhibitor of AGEs.

Key words： hydroxysafflor yellow A; advanced glycation end products; fluorescence spectroscopy; molecular docking

Cite this article

WANG Jiamin , ZHANG Bohui , WANG Laizhong , GUO Limin , BAO Xiaowei . Inhibitory effect of hydroxysafflor yellow A on formation of advanced glycation end products[J]. Food and Fermentation Industries, 2026 , 52(12) : 161 -167 . DOI: 10.13995/j.cnki.11-1802/ts.044397

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