Probing the binding interaction of thionine with lysozyme: A spectroscopic and molecular docking investigation

被引：84

作者：

Shanmugaraj, Krishnamoorthy ^{[1
]}

Anandakumar, Shanmugam ^{[2
]}

Ilanchelian, Malaichamy ^{[1
]}

机构：

[1] Bharathiar Univ, Dept Chem, Coimbatore 641046, Tamil Nadu, India

[2] Bharathiar Univ, Dept Bioinformat, Coimbatore 641046, Tamil Nadu, India

来源：

DYES AND PIGMENTS | 2015年 / 112卷

关键词：

Lysozyme; Thionine; Emission; Circular dichroism; Three dimensional emission spectroscopy; Molecular docking; HUMAN SERUM-ALBUMIN; TOLUIDINE BLUE O; METHYLENE-BLUE; PHENOTHIAZINIUM DERIVATIVES; PHOTOBACTERICIDAL ACTIVITY; CONFORMATIONAL-CHANGES; DRUG-THERAPY; FLUORESCENCE; PROTEIN; NANOPARTICLES;

D O I：

10.1016/j.dyepig.2014.07.003

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

In this article, an attempt is made to explore the binding mechanism of thionine with lysozyme by using multi-spectroscopic and molecular docking methods. The results from emission and time resolved fluorescence studies revealed that the emission quenching of lysozyme with thionine is initiated by static quenching mechanism. The binding constant and number of binding site of lysozyme thionine complex was evaluated as 4.01 x 10(5) dm(3) mol(-1) and approximate to 1, respectively. Furthermore, the results from absorption, constant wavelength synchronous fluorescence, three dimensional emission and circular dichroism spectral studies showed that thionine induced conformational changes in the secondary structure of lysozyme. Molecular docking study confirmed that the probable binding site of thionine is located near trptophan-63 residue of lysozyme and it is further revealed that the existence of hydrogen bonding along with hydrophobic interaction are the primary forces responsible for the complexation of thionine with lysozyme. (C) 2014 Elsevier Ltd. All rights reserved.

引用

页码：210 / 219

页数：10

共 59 条

[1] Binding of Hydroxyquinoline Probes to Human Serum Albumin: Combining Molecular Modeling and Forster's Resonance Energy Transfer Spectroscopy to Understand Flexible Ligand Binding [J].