Molecular docking and spectroscopic study of bovine serum albumin interaction with new anticancer Pt complex with isopentyl dithiocarbamate ligand

Abstract

Although cisplatin is useful in the treatment of cancer, it has a series of side effects that limit its use. Dithiocarbamates reduce the toxicity of platinum due to their structure and the presence of S, and N donating groups. In this article, the interaction of [Pt(bpy)(isopentyl.dtc)]NO₃, where bpy is bipyridine and isopentyl.dtc is isopentyl-dithiocarbamate, with BSA, bovine serum albumin has been studied. The molecular binding method, including UV-Vis and fluorescence titration, was carried out in conditions including pH = 7.4 and temperatures of 27 and 37 °C. The negative values of enthalpy (ΔH°_b) and entropy (ΔS°_b) show that the driving forces of this interaction are hydrogen and van der Waals, and the negative value of the Gibbs free energy, ΔG°_b indicates that the interaction proceeds spontaneously. The fluorescence results showed that the quenching mechanism is the static type and the Stern Volmer constant, K_SV, was also obtained. The fluorescence titration method data displayed that the quenching mechanism is static. Binding constant (K_b), binding point (n), Hill coefficients, n_H, Hill constant, K_H, number of binding sites, g, BSA melting temperature, Tm, were also obtained. Finally, the molecular docking method result shows the binding constant, K_i and binding free energy for the platinum complex are −6.53 and 16.39 kcal mol⁻¹, respectively, and also the proper position of binding on BSA can be considered the site I in the subdomain IIA.

Graphical Abstract

Keywords:

• Anticancer Pt compound
• bovine serum albumin
• docking simulation

Acknowledgments

We are thankful to the Research Council of Payame Noor University for their fiscal support.

Disclosure statement

No potential conflict of interest was reported by the authors.

Ethics approval

This article does not contain any studies with human participants or animals performed by any of the authors.

Author contributions

All authors, Z. Arabpour S., N. Sohrabi, M. Eslami Moghadam, and M. Oftadeh analyzed and interpreted the data and wrote the article. Also, N. Sohrabi and M. Eslami Moghadam read and approved the final manuscript.

Consent for publication

Authors have an agreement for publishing data before submitting the paper to this journal.

Data availability statement

All data generated or analyzed during this study are included in this published article.

Additional information

Funding

The work was supported by Payame Noor University.