Spectroscopic and calorimetric studies of interaction of methimazole with human serum albumin

被引：58

作者：

Afrin, Sadaf ^{[1
]}

Riyazuddeen ^{[1
]}

Rabbani, Gulam ^{[2
]}

Khan, Rizwan Hasan ^{[2
]}

机构：

[1] Aligarh Muslim Univ, Dept Chem, Aligarh 202002, Uttar Pradesh, India

[2] Aligarh Muslim Univ, Interdisciplinary Biotechnol Unit, Aligarh 202002, Uttar Pradesh, India

来源：

JOURNAL OF LUMINESCENCE | 2014年 / 151卷

关键词：

Antithyroid drug; Methimazole; Human serum albumin; Fluorescence spectroscopy; Isothermal titration calorimetry; DRUG BINDING-SITES; CRYSTAL-STRUCTURE; LIGAND-BINDING; PROTEIN; BOVINE; HYPERTHYROIDISM; THERMODYNAMICS; RESOLUTION;

D O I：

10.1016/j.jlumin.2014.02.028

中图分类号：

O43 [光学];

学科分类号：

070207 ; 0803 ;

摘要：

The interaction of the anti-thyroid drug, 2-mercapto 1-methylimidazole (methimazole) with human serum albumin (HSA) has been examined by fluorescence and isothermal titration calorimetry (ITC) techniques. Fluorescence results indicate that in case of HSA-drug complex the quenching of fluorescence intensity is at 340 nm. The methimazole has an ability to quench the intrinsic fluorescence of HSA tryptophan through a static quenching procedure. The binding constant has been determined using Stern-Volmer modified equation and energy transfer mechanisms of quenching are discussed. The Delta G degrees, Delta H degrees, and Delta S degrees values are also calculated by ITC measurements. The experimental spectroscopic and thermodynamic parameters have been used for understanding the binding mechanism of anti-thyroid drug with HSA. (C) 2014 Elsevier B.V. All rights reserved.

引用

页码：219 / 223

页数：5

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