Interaction study of pioglitazone with albumin by fluorescence spectroscopy and molecular docking

被引：85

作者：

Faridbod, Farnoush ^{[2
]}

Ganjali, Mohammad Reza ^{[1
]}

Larijani, Bagher ^{[1
]}

Riahi, Siavash ^{[2
,3
]}

Saboury, Ali Akbar ^{[4
]}

Hosseini, Morteza ^{[5
]}

Norouzi, Parviz ^{[1
]}

Pillip, Christoph ^{[1
]}

机构：

[1] Univ Tehran, Fac Chem, Ctr Excellence Electrochem, Tehran, Iran

[2] Univ Tehran Med Sci, Endocrinol & Metab Res Ctr, Tehran, Iran

[3] Univ Tehran, Fac Engn, Inst Petr Engn, Tehran, Iran

[4] Univ Tehran, Inst Biochem & Biophys, Tehran, Iran

[5] Islamic Azad Univ, Dept Chem, Savadkooh Branch, Savadkooh, Iran

来源：

SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY | 2011年 / 78卷 / 01期

关键词：

Fluorescence quenching; Pioglitazone; Human serum albumin; Molecular docking study; HUMAN SERUM-ALBUMIN; BINDING; FORCES;

D O I：

10.1016/j.saa.2010.09.001

中图分类号：

O433 [光谱学];

学科分类号：

070207 [光学];

摘要：

Pioglitazone is a medicine of thiazolidinedione (TZD) class with hypoglycemic (antihyperglycemic, antidiabetic) action. Pioglitazone binding to human serum albumin (HSA) was investigated at different temperatures (290, 300 and 310 K) by fluorescence spectroscopic method. Molecular docking study was also carried out besides the experiments. Experimental results revealed that pioglitazone have an ability to quench the intrinsic fluorescence of HSA tryptophan through a static quenching procedure. The binding constant was determined using Stern-Volmer modified equation and energy transfer mechanisms of quenching were discussed. Thermodynamic parameters were also calculated according to enthalpy changes dependence on different temperatures. According to the theoretical and experimental results, hydrogen bonding was found to play a major role in the interaction of pioglitazone with HSA. (C) 2010 Elsevier B.V. All rights reserved.

引用

页码：96 / 101

页数：6

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