Spectroscopic and molecular docking studies on interaction of two Schiff base complexes with bovine serum albumin

被引：15

作者：

Dezhampanah, Hamid ^{[1
]}

Esmaili, Masoomeh ^{[1
]}

Jampour, Shabnam ^{[1
]}

机构：

[1] Univ Guilan, Fac Sci, Dept Chem, POB 41335-1914, Rasht 0098, Iran

来源：

JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS | 2020年 / 38卷 / 09期

关键词：

Bovine serum albumin; ternary amino acid Schiff base-phenantrotline Cu(II); Docking study; Forster energy transfer; molecular modeling; AMINO-ACIDS; X-RAY; BINDING; BSA; DFT;

D O I：

10.1080/07391102.2019.1639548

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

This study was designed to examine interaction of two ternary copper (II) Schiff base complexes with bovine serum albumin (BSA), using spectroscopic and molecular docking techniques. The fluorescence quenching measurements revealed that the quenching mechanism was static and the binding site of both Schiff bases to BSA was singular. Forster energy transfer measurements, synchronous fluorescence spectroscopy, and docking study showed both Schiff bases bind to the Trp residues of BSA in short distances. Docking study showed that both Schiff base molecules bind with BSA by forming several hydrogen and van der Waals bonds. In addition, molecular docking study indicated that Schiff base A and Schiff base B were located within the binding pocket of subdomain IB and subdomain IIA of BSA, respectively. Results of Fourier transform-infrared spectroscopy demonstrated that bovine serum albumin interacts with both Schiff bases and the secondary structure of BSA was changed. Communicated by Ramaswamy H. Sarma

引用

页码：2650 / 2658

页数：9

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