Interaction of  Rhein-Cu(Ⅱ) Complexes with Bovine Serum Albumin

Chem. J. Chinese Universities ›› 2011, Vol. 32 ›› Issue (6): 1277.

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Interaction of Rhein-Cu(Ⅱ) Complexes with Bovine Serum Albumin

ZHAO Fang^1*, LIANG Hui¹, CHENG Hui¹, WANG Jun¹, ZHAO Wen-Hui²

1. Xinjiang Bingtuan Key Laboratory of Chemical Engineering for Green Process, College of Chemistry and Chemical Engineering, Shihezi University, Shihezi 832003, China;
2. School of Pharmacy, Xinjiang Medical University, Urumqi 830054, China

Received:2010-07-23 Revised:2010-10-15 Online:2011-06-10 Published:2011-05-10
Contact: ZHAO Fang E-mail:nnllzzff@163.com
Supported by:
国家自然科学基金(批准号: 20961009)资助.

Abstract

Abstract: The interaction between rhein-Cu and bovine serum albumin(BSA) was investigated by fluorescence and ultraviolet spectroscopy. The results indicated that rhein-Cu led to the intrinsic fluorescence quenching of BSA through a static quenching procedure. The binding constants KA and binding site n at 298 K and 309 K were obtained. The binding locality was found to be an area 3.24 nm away from tryptophan residue in BSA based on F?rster non-radiation energy transfer mechanism. The experimental results showed that the rhein-Cu could be inserted into the BSA, quenching the inner fluorescence by forming the rhein-Cu-BSA complex. The binding power between rhein-Cu and BSA is mainly the hydrophobic interaction according to the thermodynamic parameters. The effect of rhein-Cu on the conformation of BSA was analyzed by circular dichroism(CD) and synchronous fluorescence spectra.

Key words: Rhein-Cu, Bovine serum albumin(BSA), Fluorescence spectrum, Ultraviolet spectrum, Circular dichroism spectrum

TrendMD:

ZHAO Fang*, LIANG Hui, CHENG Hui, WANG Jun, ZHAO Wen-Hui. Interaction of Rhein-Cu(Ⅱ) Complexes with Bovine Serum Albumin[J]. Chem. J. Chinese Universities, 2011, 32(6): 1277.

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Interaction of Rhein-Cu(Ⅱ) Complexes with Bovine Serum Albumin

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