牛血清白蛋白
化学
抗氧化剂
猝灭(荧光)
DPPH
氢键
疏水效应
血清白蛋白
色谱法
生物化学
荧光
生物物理学
有机化学
分子
生物
物理
量子力学
作者
Shu-Fen Wu,Xiaochan Wang,Yuxin Bao,Chuanying Zhang,Huanhuan Liu,Zhenjing Li,Mianhua Chen,Changlu Wang,Qingbin Guo,Xin Peng
出处
期刊:Food Chemistry
[Elsevier]
日期:2020-06-01
卷期号:315: 126228-126228
被引量:35
标识
DOI:10.1016/j.foodchem.2020.126228
摘要
Monascin (MS) is a yellow lipid-soluble azaphilonoid pigment identified from Monascus-fermented products with promising biological activities. This work studied interactions between MS and bovine serum albumin (BSA) as well as their influences on the antioxidant activity of MS. Experimental results demonstrated that the fluorescence emission of BSA was quenched by MS via static quenching mechanism and the formed BSA-MS complex was mainly maintained by hydrophobic and hydrogen bond interactions. Meanwhile, the probable binding pocket of MS located near site I of BSA and the corresponding conformational and structural alterations of BSA were determined. Furthermore, the molecular modeling approach was performed to understand the visual representation of binding mode between BSA and MS. It was noticeable that the BSA-MS complex exhibited reduced DPPH radical-scavenging ability, which might be attributed to the restraining effect of BSA on the relevant reaction pathways involved in antioxidation by MS.
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