Comparison of Protective Effects of Phenolic Acids on Protein Glycation of BSA Supported by In Vitro and Docking Studies

Marzieh Rashedinia; Zeinab Rasti Arbabi; Razieh Sabet; Leila Emami; Alireza Poustforoosh; Zahra Sabahi

doi:10.1155/2023/9984618

Comparison of Protective Effects of Phenolic Acids on Protein Glycation of BSA Supported by In Vitro and Docking Studies

Biochem Res Int. 2023 Jul 18:2023:9984618. doi: 10.1155/2023/9984618. eCollection 2023.

Authors

Marzieh Rashedinia^{1

2

3}, Zeinab Rasti Arbabi³, Razieh Sabet⁴, Leila Emami⁵, Alireza Poustforoosh⁶, Zahra Sabahi^{1

2}

Affiliations

¹ Food and Supplements Safety Research Center, Shiraz University of Medical Sciences, Shiraz, Iran.
² Medicinal Plants Processing Research Center, Shiraz University of Medical Sciences, Shiraz, Iran.
³ Department of Pharmacology and Toxicology, School of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran.
⁴ Department of Medicinal Chemistry, Faculty of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran.
⁵ Pharmaceutical Sciences Research Center, Shiraz University of Medical Sciences, Shiraz, Iran.
⁶ Medicinal and Natural Products Chemistry Research Center, Shiraz University of Medical Sciences, Shiraz, Iran.

Abstract

Several diabetic complications are associated with forming advanced glycation end products (AGEs). Different chemical and natural compounds are able to prevent the development of these products. In this study, glycosylation was induced as a model by incubating bovine serum albumin (BSA) with glucose. Consequently, BSA was treated with glucose and different concentrations (1.25, 2.5, and 5 μM) of syringic acid, gallic acid, ellagic acid, ferulic acid, paracoumaric acid, and caffeic acid for 4 and 6 weeks. Biochemical experiments comprise measurements of fluorescent AGEs, protein carbonyl contents, total thiol, hemolysis tests, and also malondialdehyde (MDA) levels in RBC. These demonstrated the antiglycating mechanism of these phenolic acids. Most of the phenolic acids used in this study reduced MDA levels and protected thiol residues in protein structures. They also inhibited the formation of fluorescent AGEs and RBC lysis, except gallic acid. Moreover, ferulic acid, paracoumaric acid, and caffeic acid proteins significantly prevent carbonylation. Molecular docking and simulation studies showed that ellagic, caffeic, gallic, and syringic acids could interact with lysine and arginine residues in the active site of BSA and stabilize its structure to inhibit the formation of AGEs. Our results suggest that phenolic acid could be used as a potential phytochemical against protein glycation and related diabetic complications.