Investigation of the interaction between amodiaquine and human serum albumin by fluorescence spectroscopy and molecular modeling

被引：124

作者：

Samari, Fayezeh ^{[1
]}

Shamsipur, Mojtaba ^{[2
]}

Hemmateenejad, Bahram ^{[1
]}

Khayamian, Taghi ^{[3
]}

Gharaghani, Sajjad ^{[3
]}

机构：

[1] Shiraz Univ, Dept Chem, Shiraz 71454, Fars, Iran

[2] Razi Univ, Dept Chem, Kermanshah, Iran

[3] Isfahan Univ Technol, Sch Chem, Isfahanm, Iran

来源：

EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY | 2012年 / 54卷

关键词：

Human serum albumin; Amodiaquin; Fluorescence; Binding; Molecular modeling; PROTEIN-LIGAND INTERACTIONS; BINDING; COMPLEXES; DYNAMICS; SIMULATION; ACID; DERIVATIVES; WARFARIN;

D O I：

10.1016/j.ejmech.2012.05.007

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

The interaction of amodiaquine (AQ) with human serum albumin (HSA) has been studied by fluorescence spectroscopy. Based on the sign and magnitude of the enthalpy and entropy changes (Delta H-0 = -43.27 kJ mol(-1) and as Delta S-0 = -50.03 J mol(-1) K-1), hydrogen bond and van der Waals forces were suggested as the main interacting forces. Moreover, the efficiency of energy transfer and distance between HSA and acceptor AQ was calculated. Finally, the binding of AQ to HSA was modeled by molecular docking and molecular dynamic simulation methods. Excellent agreement was found between the experimental and theoretical results. Both experimental results and modeling methods suggested that AQ binds mainly to the sub-domain IIA of HSA. (c) 2012 Elsevier Masson SAS. All rights reserved.

引用

页码：255 / 263

页数：9

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