Effect of pH on the Interaction of Lutein with Bovine Serum Albumin Studied by Fluorescence Spectroscopy

被引：1

作者：

Fan J. ^{[1
]}

Kang Z. ^{[1
]}

Zhang Y. ^{[1
]}

Su D. ^{[1
]}

Zhou S. ^{[1
]}

Lü C. ^{[1
]}

机构：

[1] Food Safety Key Laboratory of Liaoning Province, National & Local Joint Engineering Research Center of Storage, Processing and Safety Control Technology for Fresh Agricultural and Aquatic Products, College of Food Science and Technology, Bohai University,

来源：

Shipin Kexue/Food Science | 2022年 / 43卷 / 16期

关键词：

Bovine serum albumin; Fluorescence spectroscopy; Lutein; Molecular simulation; PH;

D O I：

10.7506/spkx1002-6630-20211025-269

中图分类号：

学科分类号：

摘要：

The interaction between lutein and bovine serum albumin (BSA) was investigated using fluorescence emission spectroscopy under different pH (3.0, 5.0 and 7.4) conditions. The quenching constant and thermodynamic parameters were calculated using a mathematical model. The fluorescence quenching and conformation changes of BSA were analyzed, and the binding sites were determined by site marker competitive experiments and molecular docking. Fluorescence spectra showed that lutein had a fluorescence quenching effect on BSA under different pH conditions. The quenching constant was the highest and the binding constant was larger at pH 7.4 and 298 K. The thermodynamic parameters and molecular docking showed that the binding of lutein with BSA was mainly driven by hydrophobic interaction. Synchronous fluorescence spectra indicated that lutein and the change of pH jointly induced the conformational changes of BSA. The results of site marker competitive experiments and molecular docking showed that the binding site of lutein and BSA was located between subdomains IIA and IIIA, but closer to Sudlow's site II at pH 7.4 and 5.2. At pH 3.0, the binding site was neither near subdomain IIA nor near subdomain IIIA. Altogether, the results revealed that pH influenced the binding of lutein and BSA, which may provide a theoretical basis for understanding the interaction between proteins and bioactive components. © 2022, China Food Publishing Company. All right reserved.

引用

页码：153 / 159

页数：6

共 23 条

[1] (2019)
[2] (2020)
[3] SUKOWSKA A., Interaction of drugs with bovine and human serum albumin, Journal of Molecular Structure, 614, pp. 227-232, (2002)
[4] RANJEET P, JENNIFER A T, CLINT R, Et al., Protein bindings and stability of drug candidates: the achilles' heel in in vitro potency assays, European Journal of Drug Metabolism and Pharmacokinetics, 45, 4, pp. 427-432, (2020)
[5] QI H Y, WANG Y, WANG X W, Et al., The different interactions of two anticancer drugs with bovine serum albumin based on multispectrum method combined with molecular dynamics simulations, Spectrochimica Acta Part A: Molecular and Biomoleculai Spectroscopy, 259, (2021)
[6] TANG N, LIU J C, CHENG Y Q., Effects of zinc binding on the binding of epigallocatechin gallate (green tea) to bovine serum albumin and myoglobin, Food Chemistry, 357, (2021)
[7] (2021)
[8] (2021)
[9] WEIGEL F, WEISS J, DECKER E A, Et al., Lutein-enriched emulsionbased delivery systems: influence of emulsifiers and antioxidants on physical and chemical stability, Food Chemistry, 242, 3, pp. 395-403, (2018)
[10] TROTT O, OLSON A J., Software news and update autodock vina:improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading, Journal of Computational Chemistry, 31, 2, pp. 455-461, (2010)

← 1 2 3 →