Spectroscopic studies on the interaction of mimosine with BSA and DNA

被引：20

作者：

Baltazar, C. J. ^{[1
]}

Mun, R. ^{[1
]}

Tajmir-Riahi, H. A. ^{[2
]}

Bariyanga, J. ^{[1
]}

机构：

[1] Univ Hawaii West Oahu, Div Humanities Math Sci, Kapolei, HI 96707 USA

[2] Univ Quebec Trois Rivieres, Dept Chem Biochem, Trois Rivieres, PQ G9A 5H7, Canada

来源：

JOURNAL OF MOLECULAR STRUCTURE | 2018年 / 1161卷

基金：

美国国家科学基金会;

关键词：

Bovine serum albumin; Deoxyribonucleic acid; Mimosine; Spectroscopy; Interaction; BOVINE SERUM-ALBUMIN; HUMAN HEMOGLOBIN PROTEINS; MOLECULAR DOCKING; BINDING INTERACTION; FT-IR; REPLICATION; COMPLEXES; CELLS; SECONDARY; DRUGS;

D O I：

10.1016/j.molstruc.2018.01.039

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Mimosine has shown antitumor activity towards cancer cells. It has also been found to inhibit deoxyribonucleic acid (DNA) but the interaction is not fully understood. Here we report the results of investigation of its interactions with bovine serum albumin (BSA) and DNA in aqueous solution (pH 7.4) using FTIR and UV spectroscopic methods. Mimosine was found to disrupt the conformation of BSA by reducing its a-helix component and promoting a partial unfolding of the protein. In addition, the results indicated that mimosine may bind to DNA by electrostatic attractions via phosphate groups and grooves. The overall binding constant of DNA mimosine complex was 5 x 10(3) M-1. (C) 2018 Elsevier B.V. All rights reserved.

引用

页码：273 / 278

页数：6

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