Spectrometric study of the interaction between Alpinetin and bovine serum albumin using chemometrics approaches

被引:132
作者
Ni, Yongnian [1 ,2 ]
Wang, Shuangshuang [2 ]
Kokot, Serge [3 ]
机构
[1] Nanchang Univ, Dept Chem, State Key Lab Food Sci & Technol, Nanchang 330047, Jiangxi, Peoples R China
[2] Nanchang Univ, Dept Chem, Nanchang 330047, Jiangxi, Peoples R China
[3] Queensland Univ Technol, Sch Phys & Chem Sci, Brisbane, Qld 4001, Australia
关键词
Alpinetin; Bovine serum albumin; Fluorescence and UV-visible spectroscopy; Chemometrics; Ligand comparison; MULTIVARIATE CURVE RESOLUTION; BINDING; ACID; HYDROCHLORIDE; FLAVONOIDS; MIXTURES; PROTEIN; RANK;
D O I
10.1016/j.aca.2010.01.053
中图分类号
O65 [分析化学];
学科分类号
070302 [分析化学];
摘要
The binding interaction of Alpinetin (APT) with bovine serum albumin (BSA) was studied by fluorescence, UV-visible and synchronous fluorescence spectroscopy (SFS) under simulated physiological conditions. The measured complex spectra were resolved by multivariate curve resolution-alternating least squares (MCR-ALS), yielding a host of data and information, which otherwise would have been impossible to obtain. The extracted profiles corresponded to the spectra of the single species in the APT/BSA mixture. In addition, the presence of the APT-BSA complex was demonstrated, and it was shown that the associated quenching of the fluorescence from the BSA protein resulted from the formation of APT-BSA complex via a static mechanism. The binding constant (K-a(ave) = 2.34 x 10(6) L mol(-1)) and the number of sites (n = 1) were obtained by fluorescence methods as were the thermodynamic parameters (Delta H-0, Delta S-0 and Delta G(0)). This work suggested that the principal binding between APT to BSA was facilitated by hydrophobic interactions. The thermodynamic parameters for APT were compared to those from the structurally similar Chrysin and Wogonin molecules. It appeared that the entropy parameters were relatively more affected by the small structural changes. SFS from the interaction of BSA and APT showed that the ligand affected the conformation of BSA. The competitive interaction of APT and site makers with BSA indicated site I as the binding area of APT in BSA. (C) 2010 Elsevier B.V. All rights reserved.
引用
收藏
页码:139 / 146
页数:8
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