期刊
FOOD RESEARCH INTERNATIONAL
卷 157, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.foodres.2022.111358
关键词
Human serum albumin; Glycation; Glyoxal; Ribose; Flavonoids
资金
- Council of Scientific & Industrial Research (CSIR, Gov't of India) [01/2903/17/EMR-II]
This study investigated the effects of two flavonoids, naringin and naringenin, on inhibiting glycation and AGEs formation of HSA, with naringenin showing stronger antiglycating potential than naringin due to better interactions with HSA.
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.
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