| Literature DB >> 31637788 |
Jianli Liu1, Zhijun Yang1, Ye Cheng1, Qiong Wu2, Yin He1, Qijiu Li1, Xiangyu Cao1.
Abstract
Maillard reaction occurs between the carbonyl group of reducing sugars and the free amino groups of protein, which eventually results in the formation and accumulation of advanced glycation end products (AGEs) irreversibly. Excessive production of AGEs is associated with many diseases, such as Alzheimer disease, neuropathy, retinopathy, and nephropathy. In this study, the effects of eriodictyol and naringenin on the inhibition of AGEs were studied with bovine serum albumin (BSA)-methylglyoxal (MGO) model by spectroscopic techniques and molecular docking methods. The fluorescence spectroscopy results suggested that eriodictyol and naringenin could inhibit the formation of AGEs. Circular dichroism (CD) studies indicated that eriodictyol and naringenin could stabilize the structure of BSA and inhibit the formation of AGEs. The molecular docking results demonstrated that eriodictyol formed two hydrogen bonds with Lys 350 and Leu 480 and the main forces were hydrogen bonding and hydrophobic interactions. However, naringenin interacted with Arg 484 of BSA, and the main force was hydrophobic interaction. It can be concluded that eriodictyol and naringenin can inhibit the formation of AGEs and eriodictyol has stronger inhibitory activity of AGEs than that of naringenin, which is probably due to the additional hydroxyl group in the position C-3' of B ring of eriodictyol.Entities:
Keywords: advanced glycation end products; eriodictyol; molecular docking; naringenin; spectroscopic studies
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Year: 2019 PMID: 31637788 DOI: 10.1002/jmr.2814
Source DB: PubMed Journal: J Mol Recognit ISSN: 0952-3499 Impact factor: 2.137