Characterization of the interaction between a platinum(II) complex and human serum albumin: spectroscopic analysis and molecular docking
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  • 作者:Somaye Shahraki ; Fereshteh Shiri…
  • 关键词:Human serum albumin ; Pt(II) complex ; Multispectroscopic methods ; Molecular docking
  • 刊名:Journal of the Iranian Chemical Society
  • 出版年:2016
  • 出版时间:April 2016
  • 年:2016
  • 卷:13
  • 期:4
  • 页码:723-731
  • 全文大小:1,331 KB
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  • 作者单位:Somaye Shahraki (1)
    Fereshteh Shiri (1)
    Hassan Mansouri-Torshizi (2)
    Jafar Shahraki (3)

    1. Department of Chemistry, University of Zabol, Zabol, Iran
    2. Department of Chemistry, University of Sistan and Baluchestan, Zahedan, Iran
    3. Department of Pharmacology and Toxicology, Faculty of Pharmacy, Zabol University of Medical Sciences, Zabol, Iran
  • 刊物主题:Analytical Chemistry; Inorganic Chemistry; Physical Chemistry; Biochemistry, general; Organic Chemistry;
  • 出版者:Springer Berlin Heidelberg
  • ISSN:1735-2428
文摘
In this study, the interaction between (2,2ʹ-bipyridine)(pyrrolidinedithiocarbamato) platinum(II) nitrate, [Pt(bpy)(pyr-dtc]NO3, and human serum albumin (HSA) was investigated by various spectroscopic methods (UV–vis, fluorescence, CD and FT-IR) and molecular docking technique at three temperatures. UV–vis absorption spectroscopy showed that Pt(II) complex can denature the protein at moderate concentrations. The results of emission quenching at two temperatures has revealed that the quenching mechanism of Pt(II) complex with HSA was static quenching mechanism. Binding constants (K), binding site number (n) and corresponding thermodynamic parameters ∆G˚, ∆H˚ and ∆S˚ were calculated and revealed that hydrophobic forces played a major role when Pt(II) complex interacted with HSA. The binding distance (r) between above complex and HSA based on Försterʼs theory of non-radiation energy transfer was calculated as 3.22 nm. Alterations of HSA secondary structure induced by complex were confirmed by FT-IR and CD measurements. Also, a molecular docking study was performed for identification of key structural features of binding of the Pt complex into the receptor and predicting bioactive conformers. Our results may provide valuable information to understand the mechanistic pathway of drug delivery and to pharmacological behavior of drug. Keywords Human serum albumin Pt(II) complex Multispectroscopic methods Molecular docking

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