Exploring the Mechanism of Fluorescence Quenching in Proteins Induced by Tetracycline

被引：148

作者：

Anand, Uttam ^{[1
]}

Jash, Chandrima ^{[1
]}

Boddepalli, Ravi Kiran ^{[1
]}

Shrivastava, Aseem ^{[1
]}

Mukherjee, Saptarshi ^{[1
]}

机构：

[1] Indian Inst Sci Educ & Res, Dept Chem Sci, Bhopal ITI Campus,Gas Rahat Bldg, Bhopal 462023, Madhya Pradesh, India

来源：

JOURNAL OF PHYSICAL CHEMISTRY B | 2011年 / 115卷 / 19期

关键词：

HUMAN SERUM-ALBUMIN; BINDING; LYSOZYME; ANTIBIOTICS; TRYPTOPHAN; RESIDUES;

D O I：

10.1021/jp2008978

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The binding of the antibiotic tetracycline hydrochloride (TC) to three proteins was investigated by steady-state, time-resolved, and circular dichroism spectroscopy. The tryptophan (Trp) amino acid residues were used as an intrinsic fluorophore to decipher the structure-function relationship. As monitored by CD spectroscopy, the addition of TC causes the protein to alter some of its helical content although such changes are only marginal. The gradual decrease in fluorescence intensity of Trp can be ascribed to static quenching which takes place by the interaction of the drug with the protein. Besides Trp quenching, there is evidence of fluorescence resonance energy transfer (FRET) in all three proteins with different values of efficiency of energy transfer. Various quenching/binding and thermodynamic parameters associated with such drug-protein interactions have been estimated. The results thus obtained can provide guidelines to synthetic chemists to design and synthesize target-oriented drugs.

引用

页码：6312 / 6320

页数：9

共 40 条

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