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The binding assessment with human serum albumin of novel six-coordinate Pt(IV) complexes, containing bidentate nitrogen donor/methyl ligands
The interactions between platinum complexes and human serum albumin (HSA) play crucial roles in the distribution, metabolism, and activity of platinum-based anticancer drugs. Octahedral platinum (IV) complexes represent a significant class of anticancer agents that display molecular pharmacological...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Shiraz University
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5019209/ https://www.ncbi.nlm.nih.gov/pubmed/27844009 |
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author | Yousefi, Reza Taheri-Kafrani, Asghar Nabavizadeh, Sayed Masoud Pouryasin, Zahra Shahsavani, Mohammad Bagher Khoshaman, Kazem Rashidi, Mehdi |
author_facet | Yousefi, Reza Taheri-Kafrani, Asghar Nabavizadeh, Sayed Masoud Pouryasin, Zahra Shahsavani, Mohammad Bagher Khoshaman, Kazem Rashidi, Mehdi |
author_sort | Yousefi, Reza |
collection | PubMed |
description | The interactions between platinum complexes and human serum albumin (HSA) play crucial roles in the distribution, metabolism, and activity of platinum-based anticancer drugs. Octahedral platinum (IV) complexes represent a significant class of anticancer agents that display molecular pharmacological properties different from cisplatin. In this study, the interaction between two Pt(IV) complexes with the general formula [Pt(X)2Me2 (tbu2bpy)], where tbu2bpy = 4,4′-ditert-butyl-2,2′-bipyridine, with two leaving groups of X = Cl (Com1) or Br (Com2), and HSA were investigated, using Ultraviolet-Visible (UV-Vis) spectroscopy, fluorescence spectroscopy, circular dichroism (CD) and molecular docking simulation. The spectroscopic and thermodynamic data revealed that the HSA/Pt(IV) complexes interactions were spontaneous process and Com2 demonstrated stronger interaction and binding constant in comparison with Com1. Also, the results suggest approximately similar structural alteration of HSA in the presence of these Pt complexes. Molecular docking revealed that both Pt(IV) complexes bind with HSA in subdomain IB, literally the same as each other. This study suggests that variation in the leaving group, displaying differing departure rate, has no significant contribution in denaturing prosperities of the Pt(IV) complexes against HSA. |
format | Online Article Text |
id | pubmed-5019209 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Shiraz University |
record_format | MEDLINE/PubMed |
spelling | pubmed-50192092016-11-14 The binding assessment with human serum albumin of novel six-coordinate Pt(IV) complexes, containing bidentate nitrogen donor/methyl ligands Yousefi, Reza Taheri-Kafrani, Asghar Nabavizadeh, Sayed Masoud Pouryasin, Zahra Shahsavani, Mohammad Bagher Khoshaman, Kazem Rashidi, Mehdi Mol Biol Res Commun Original Article The interactions between platinum complexes and human serum albumin (HSA) play crucial roles in the distribution, metabolism, and activity of platinum-based anticancer drugs. Octahedral platinum (IV) complexes represent a significant class of anticancer agents that display molecular pharmacological properties different from cisplatin. In this study, the interaction between two Pt(IV) complexes with the general formula [Pt(X)2Me2 (tbu2bpy)], where tbu2bpy = 4,4′-ditert-butyl-2,2′-bipyridine, with two leaving groups of X = Cl (Com1) or Br (Com2), and HSA were investigated, using Ultraviolet-Visible (UV-Vis) spectroscopy, fluorescence spectroscopy, circular dichroism (CD) and molecular docking simulation. The spectroscopic and thermodynamic data revealed that the HSA/Pt(IV) complexes interactions were spontaneous process and Com2 demonstrated stronger interaction and binding constant in comparison with Com1. Also, the results suggest approximately similar structural alteration of HSA in the presence of these Pt complexes. Molecular docking revealed that both Pt(IV) complexes bind with HSA in subdomain IB, literally the same as each other. This study suggests that variation in the leaving group, displaying differing departure rate, has no significant contribution in denaturing prosperities of the Pt(IV) complexes against HSA. Shiraz University 2015-12 /pmc/articles/PMC5019209/ /pubmed/27844009 Text en This is an Open Access article distributed under the terms of the Creative Commons Attribution License, (http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Article Yousefi, Reza Taheri-Kafrani, Asghar Nabavizadeh, Sayed Masoud Pouryasin, Zahra Shahsavani, Mohammad Bagher Khoshaman, Kazem Rashidi, Mehdi The binding assessment with human serum albumin of novel six-coordinate Pt(IV) complexes, containing bidentate nitrogen donor/methyl ligands |
title | The binding assessment with human serum albumin of novel six-coordinate Pt(IV) complexes, containing bidentate nitrogen donor/methyl ligands |
title_full | The binding assessment with human serum albumin of novel six-coordinate Pt(IV) complexes, containing bidentate nitrogen donor/methyl ligands |
title_fullStr | The binding assessment with human serum albumin of novel six-coordinate Pt(IV) complexes, containing bidentate nitrogen donor/methyl ligands |
title_full_unstemmed | The binding assessment with human serum albumin of novel six-coordinate Pt(IV) complexes, containing bidentate nitrogen donor/methyl ligands |
title_short | The binding assessment with human serum albumin of novel six-coordinate Pt(IV) complexes, containing bidentate nitrogen donor/methyl ligands |
title_sort | binding assessment with human serum albumin of novel six-coordinate pt(iv) complexes, containing bidentate nitrogen donor/methyl ligands |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5019209/ https://www.ncbi.nlm.nih.gov/pubmed/27844009 |
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