Spectroscopic Studies on the Interaction Between Rifabutin and Human Serum Albumin

Chem. J. Chinese Universities

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Spectroscopic Studies on the Interaction Between Rifabutin and Human Serum Albumin

WANG Cong-Xia, YE Ling*, YAN Fang-Fei, WANG Nan, YU Pei-Lin

School of Chemical Biology and Pharmaceutical Sciences, Capital University of Medical Sciences, Beijing 100069, China

Received:2007-03-29 Revised:1900-01-01 Online:2007-12-10 Published:2007-12-10
Contact: YE Ling

Abstract

Abstract: The binding mechanism between Rifabutin(RB) and human serum albumin(HSA) was studied by fluorescence spectroscopy and CD. The results show that RB quenched the intrinsic fluorescence of HSA via a combination of static and dynamic quenching processes and hydrophobic interaction played a major role in stabilizing the RB-HSA complex. The binding constant K_a was calculated to be in the order of 10⁶, indicating a strong interaction between RB and HSA. In addition, influences of metal ion(Cu²⁺, Zn²⁺, Mg²⁺ and Ca²⁺) on K_a were studied. Moreover, synchronous fluorescence spectroscopy and circular dichroism(CD)reveal the conformational change of HSA upon binding with RB.

Key words: Rifabutin(RB), Human serum albumin(HSA), Fluorescence spectroscopy, Circular dichroism

CLC Number:

O657

TrendMD:

WANG Cong-Xia, YE Ling*, YAN Fang-Fei, WANG Nan, YU Pei-Lin. Spectroscopic Studies on the Interaction Between Rifabutin and Human Serum Albumin[J]. Chem. J. Chinese Universities, doi: .

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Spectroscopic Studies on the Interaction Between Rifabutin and Human Serum Albumin

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