Effect of Presence of Aliphatic Glycine in the Anti-cancer Platinum Complex Structure on Human Serum Albumin Binding
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ORIGINAL ARTICLE
Effect of Presence of Aliphatic Glycine in the Anti-cancer Platinum Complex Structure on Human Serum Albumin Binding Afrooz Shiekhzadeh 1 & Nasrin Sohrabi 1 & Mahboube Eslami Moghadam 2
&
Mohsen Oftadeh 1 & Adeleh Divsalar 3
Accepted: 11 October 2020 # Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract Purpose In this work, a new water-soluble Pt(II) complex was synthesized with aliphatic glycine ligand with a formula of cis-[Pt(NH3)2(isopentylgly)]NO3, as an anti-cancer drug, and characterized. To determine the binding constant of the human serum albumin (HSA, the most abundant carrier proteins in the human circulatory system) to this complex and the binding site of the complex on HSA, the melting point of HSA and the kinetics of this interaction were investigated to introduce an anti-breast cancer drug with fewer side effects. Methods HSA interaction with the complex was studied via a spectroscopic method at 27 and 37 °C and physiological situation (I = 10 mM, pH = 7.4) and molecular docking. Results The toxicity value of this complex was obtained against the human cancer breast cell line of MCF-7. The thermodynamic parameters of enthalpy and entropy were also achieved in the empirical procedure. Due to the spontaneity of the interaction, Gibbs free energy variation was obtained negative. The binding constant of this complex to HSA was 3.9 × 105 (M−1). Empirical results showed that the quenching mechanism was static. Hill coefficients, Hill constant, complex aggregation number around protein, number of binding sites, and protein melting temperature with complex were obtained. The kinetics of this interaction was also investigated, which showed that this interaction follows a second-order kinetic. The molecular docking data indicated that the position of the interaction of complex on the protein was the site I in the subsecond IIA. Also, the hydrogen bonding and the hydrophobic interaction as the dominant binding forces were seen in complex–HSA formation. Conclusion This interaction with positive cooperativity was recognized via a superior hydrogen bond. The reasonable binding constant was also obtained, which could ultimately be a good option as an anti–breast cancer drug. Keywords Human serum albumin . Hill constant . Aggregation number . Platinum(II) complex . Molecular docking
Abbreviations HSA Human serum albumin PDB Protein Data Bank
* Nasrin Sohrabi [email protected]; [email protected] * Mahboube Eslami Moghadam [email protected]; [email protected] 1
Department of Chemistry, Payame Noor University (PNU), P.O BOX 19395-4697, Tehran, Iran
2
Chemistry & Chemical Engineering Research Center of Iran, Tehran, Iran
3
Department of cell & molecular biology, Faculty of Biological Sciences, Karazmi University, Tehran, Iran
Introduction In chemotherapy, the interaction of the anti-cancer metallodrugs with proteins especially human serum albumin (HSA) can affect the biological activity of the body [1]. The study of this significant interacti
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