Study on the interaction of three structurally related cationic Pt(II) complexes with human serum albumin: importance of binding affinity and denaturing properties
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- 作者：Reza Yousefi ; Mehrnaz Jamshidi…
- 关键词：Cationic Pt(II) complexes ; Human serum albumin ; Anticancer activity ; Fluorescence ; Circular dichroism
- 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：617-630
- 全文大小：3,660 KB
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Mehrnaz Jamshidi (1)
Mohammad Bagher Shahsavani (1)
S. Masoud Nabavizadeh (4)
Mohsen Golbon Haghighi (4) (6)
Mehdi Rashidi (4)
Asghar Taheri-Kafrani (3)
Ali Niazi (2)
Fatemeh Keshavarz (1) (5)
Mohammad Mehdi Alavinamehr (5)
1. Protein Chemistry Laboratory (PCL), Department of Biology, College of Sciences, Shiraz University, Shiraz, Iran
2. Institute of Biotechnology, Shiraz University, Shiraz, Iran
4. Department of Chemistry, College of Sciences, Shiraz University, Shiraz, Iran
6. Department of Chemistry, Shahid Beheshti University, Evin, Tehran, 19839-69411, Iran
3. Department of Biotechnology, Faculty of Advanced Sciences and Technologies, University of Isfahan, Isfahan, 81746-73441, Iran
5. Department of Chemistry, Shiraz University of Technology, Shiraz, 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
Human serum albumin (HSA) primarily functions as a transport carrier for a vast variety of natural ligands and pharmaceutical drugs. In the present study, three structurally related cationic Pt(II) complexes ([Pt(ppy)(dppe)]CF3CO2: 1, Pt(bhq)(dppe)]CF3CO2: 2, and [Pt(bhq)(dppf)]CF3CO2: 3) were used to evaluate their interaction with HSA under different experimental setups, using UV–Vis absorption spectroscopy, fluorescence and circular dichroism techniques. The spectroscopic results suggest that upon binding to HSA, the Pt(II) complexes could effectively induce structural alteration of the protein. The complexes can bind to HSA with the binding affinities of the following order: 3 > 2 > 1. Also, thermodynamic parameters of binding between these complexes and HSA indicated the existence of entropy-driven spontaneous interaction which primarily dominated with the hydrophobic forces. Also, docking simulation study revealed the binding details of these complexes on HSA. Complex 3 with highest binding affinity for HSA indicates lowest denaturing effect on this protein. The low denaturation properties of 3 appear important in the terms of lower susceptibility of this platinum complex for possible development of deleterious side effects. Keywords Cationic Pt(II) complexes Human serum albumin Anticancer activity Fluorescence Circular dichroism