Human serum albumin binding studies of a new platinum(IV) complex containing the drug pregabalin: experimental and computational methods

Abstract

A new platinum(IV) complex, [Pt(en)(Cl)₂(Pregabalin)₂], containing the drug pregabalin was synthesized and characterized by elemental analysis, FT-IR, ¹H NMR, mass spectrum, thermogravimetric analysis (TGA), molecular docking and RHF/PM6 method. Also, the interaction of Pt(IV) complex with human serum albumin (HSA) was studied by using UV–vis, fluorometric, circular dichroism (CD) spectroscopies and molecular docking techniques. The results demonstrated that the binding of the complex to HSA caused strong fluorescence quenching of HSA through static quenching mechanism. Hydrogen bonds and van der Waals contacts are the major forces in the stability of protein-Pt(IV) complex and the process of the binding of complex with HSA was enthalpy driven (ΔH = –105.8 kJ·mol⁻¹). The results of CD and UV–vis spectroscopy indicated that the binding of the complex to HSA caused conformational changes in HSA. In addition, the study of molecular docking and RHF/PM6 method confirm the experimental results with respect to the mechanism of binding.

Keywords:

• Pt(IV) complex
• human serum albumin (HSA)
• fluorescence quenching
• molecular docking
• hydrogen interaction

Disclosure statement

No potential conflict of interest was reported by the authors.

Funding

Financial support from the Razi University Research Center is gratefully acknowledged.

Additional information

Funding

Financial support from the Razi University Research Center is gratefully acknowledged