Effect of the glycosylation of flavonoids on interaction with protein

被引：81

作者：

Cao, Hui ^{[1
]}

Wu, Donghui ^{[1
]}

Wang, Hongxian ^{[1
]}

Xu, Ming ^{[2
]}

机构：

[1] Nantong Univ, Sch Chem & Chem Engn, Nantong 226007, Jiangsu, Peoples R China

[2] Mem Sloan Kettering Canc Ctr, Dept Radiat Oncol, New York, NY 10021 USA

来源：

SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY | 2009年 / 73卷 / 05期

关键词：

BSA; Flavonoid; Glycosylation; Interaction; Fluorescence quenching; BOVINE SERUM-ALBUMIN; MULTI-SPECTROSCOPIC METHOD; ANTIOXIDANT ACTIVITY; FLUORESCENCE; QUERCETIN; BINDING; ELECTROPHORESIS; PUERARIN; ACID;

D O I：

10.1016/j.saa.2009.05.004

中图分类号：

O433 [光谱学];

学科分类号：

070207 [光学];

摘要：

In this paper, two flavonoid aglycones (baicalein, quercetin) and their glycosides (baicalin, quercitrin) were studied for their ability to bind protein by quenching the protein intrinsic fluorescence. From the spectra obtained, the bimolecular quenching constants, the apparent static binding constants, and binding sites values were calculated. The glycosylation of flavonoids decreases the binding affinity with protein. For quercetin and quercitrin, the binding constants for BSA were 3.65 x 10(7) and 6.47 x 10(3) L mol(-1), respectively. For baicalein and baicalin, the binding constants were 4.54 x 10(8) and 1.63 x 10(6) L mol(-1), respectively. (C) 2009 Elsevier B.V. All rights reserved.

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页码：972 / 975

页数：4

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