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光谱和分子对接研究人血清白蛋白与铜(II)配合物的相互作用。

Spectroscopic and molecular docking studies on the interaction of human serum albumin with copper(II) complexes.

机构信息

Department of Chemistry, Jadavpur University, Kolkata, 700032, India.

Institute of Molecular Science, Key Laboratory of Chemical Biology and Molecular Engineering of the Education Ministry, Shanxi University, 92 Wucheng Road, Taiyuan, Shanxi 030006, People's Republic of China.

出版信息

Spectrochim Acta A Mol Biomol Spectrosc. 2017 Feb 15;173:740-748. doi: 10.1016/j.saa.2016.10.043. Epub 2016 Oct 23.

DOI:10.1016/j.saa.2016.10.043
PMID:27792986
Abstract

Two osazone based ligands, butane-2,3-dione bis(2'-pyridylhydrazone) (BDBPH) and hexane-3,4-dione bis(2'-pyridylhydrazone) (HDBPH), were synthesized out of the 2:1M Schiff base condensation of 2-hydrazino pyridine respectively with 2,3-butanedione and 3,4-hexanedione. The X-ray crystal structures of both the ligands have been determined. The copper(II) complex of HDBPH has also been synthesized and structurally characterized. HDBPH and its copper(II) complex have thoroughly been characterized through various spectroscopic and analytical techniques. The X-ray crystal structure of the copper complex of HDBPH shows that it is a monomeric Cu(II) complex having 'NO' co-ordination chromophore. Interaction of human serum albumin (HSA) with these ligands and their monomeric copper(II) complexes have been studied by various spectroscopic means. The experimental findings show that the ligands as well as their copper complexes are good HSA binders. Molecular docking investigations have also been done to unravel the mode of binding of the species with HSA.

摘要

两种基于肟的配体,即丁烷-2,3-二酮双(2'-吡啶基腙)(BDBPH)和己烷-3,4-二酮双(2'-吡啶基腙)(HDBPH),是通过 2-氨基吡啶分别与 2,3-丁二酮和 3,4-己二酮以 2:1M 的席夫碱缩合反应合成的。两种配体的 X 射线晶体结构均已确定。HDBPH 的铜(II)配合物也已被合成并进行了结构表征。HDBPH 及其铜(II)配合物已通过各种光谱和分析技术进行了彻底表征。HDBPH 的铜配合物的 X 射线晶体结构表明,它是具有'NO'配位发色团的单体 Cu(II)配合物。通过各种光谱手段研究了人血清白蛋白(HSA)与这些配体及其单体铜(II)配合物的相互作用。实验结果表明,配体及其铜配合物均为良好的 HSA 结合剂。还进行了分子对接研究,以揭示物种与 HSA 结合的方式。

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