Isorenieratene interaction with human serum albumin: Multi-spectroscopic analyses and docking simulation

被引:40
作者
Chen, Yashu [1 ]
Zhou, Yufeng [1 ]
Chen, Mo [2 ]
Xie, Bijun [1 ]
Yang, Jifang [3 ]
Chen, Jigang [3 ]
Sun, Zhida [1 ]
机构
[1] Huazhong Agr Univ, Dept Food Sci & Technol, Nat Prod Lab, Wuhan 430070, Hubei, Peoples R China
[2] Huazhong Agr Univ, Coll Informat, Agr Bioinformat Key Lab Hubei Prov, Wuhan, Hubei, Peoples R China
[3] Zhejiang Wanli Univ, Coll Biol & Environm Sci, Ningbo 315100, Zhejiang, Peoples R China
关键词
Isorenieratene; Human serum albumin; Fluorescence spectroscopy; Fourier transform infrared spectroscopy; Surface-enhanced Raman scattering; Docking simulation; BINDING-SITES; CAROTENOIDS; STABILITY; ASTAXANTHIN; SURFACTANTS; PROTEINS; AFFINITY; MODEL; BSA; NMR;
D O I
10.1016/j.foodchem.2018.02.105
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Isorenierantene was reported to be an aromatic carotenoid and has become a food ingredient, mainly from smear cheese, which possesses special antioxidant ability and significant photoprotective effect. In this paper, the interaction of isorenieratene with human serum albumin (HSA) was explored and compared with that of nonaromatic carotenoids using multi-spectroscopic methods and docking simulations. The results suggested isorenieratene could bind to HSA through a static quenching mechanism. The binding processes were spontaneous and exothermic, and the binding between isorenieratene and HSA was mainly driven by hydrophobic forces and electrostatic attraction. Synchronous fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, and surface-enhanced Raman scattering (SERS) experiments showed isorenieratene may change the secondary structure of HSA and the micro-environment of its amino acids. Additionally, isorenieratene showed higher stability during the binding process than did nonaromatic carotenoids. Docking simulation indicated isorenieratene may bind to HSA at site II.
引用
收藏
页码:393 / 399
页数:7
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