Mitigation of ribose and glyoxal induced glycation, AGEs formation and aggregation of human serum albumin by citrus fruit phytochemicals naringin and naringenin: An insight into their mechanism of action

被引：12

作者：

Sarmah, Sharat ^{[1
]}

Goswami, Archita ^{[1
]}

Belwal, Vinay Kumar ^{[2
]}

Roy, Atanu Singha ^{[1
]}

机构：

[1] Natl Inst Technol, Dept Chem, Shillong 793003, Meghalaya, India

[2] Indian Inst Technol Guwahati, Dept Biosci & Bioengn, Gauhati 781039, India

来源：

FOOD RESEARCH INTERNATIONAL | 2022年 / 157卷

关键词：

Human serum albumin; Glycation; Glyoxal; Ribose; Flavonoids; DRUG-BINDING-SITES; END-PRODUCTS; MAILLARD-REACTION; OXIDATIVE STRESS; CROSS-LINKING; IN-VITRO; PROTEIN GLYCATION; AMYLOID FORMATION; FLAVONOIDS; BOVINE;

D O I：

10.1016/j.foodres.2022.111358

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Human serum albumin (HSA) being the most prevalent protein in the plasma is extremely vulnerable to glycation. Two flavonoids naringin and naringenin were tested for their effects on the glyoxal and ribose-induced glycation, advanced glycation end products (AGEs) and fibril formation of HSA. The inhibition of the formation of AGEs in the presence of both flavonoids demonstrated their antiglycating properties. The presence of fibrillar aggregates in the glyoxal and ribose modified HSA were also decreased by naringin and naringenin. The explanation for naringenin's stronger antiglycating potential than naringin was further investigated by examining their interactions with HSA. H-bonding and other non-covalent interactions with flavonoids stabilize HSA. Interactions of lysine and arginine residues with flavonoids may prevent the residues from getting modified during glycation process. Naringenin bind to both subdomains IIA and IIIA of HSA, protecting more residues than naringin, which only binds to subdomain IIA, may describe the higher inhibitory activity of naringenin.

引用

页数：17