Synthesis of Two Novel Copper (II) Complexes as Potential Inhibitors of HIV-1 Protease Enzyme: Experimental and Theoretical Investigations

In this study, we report the synthesis of two new copper complexes: [Cu(C11H7O2)(SCN)(C10H8N2)], denoted as (C-1), and [Cu(C11H7O2) (C12H8N2) Cl]center dot H2O, denoted as (C-2). They are based on 2,2 '-bipyridine or 1,10-phenanthroline and 2-hydroxy-1-naphtaldehyde ligands. The obtained complexes were characterized by FT-IR, UV-visible spectroscopy, and single-crystal X-ray diffraction analysis. Molecular docking was employed to predict the binding mode involved in the interaction between the two synthetic copper (II) complexes and HIV-1 protease enzyme. The X-ray structural analysis revealed that the crystal structures of both complexes are mainly stabilized by several intra- and intermolecular hydrogen bonds. The fingerprint plots associated with the Hirshfeld surfaces of both complexes clearly show that H center dot center dot center dot H interactions provide the largest contributions. According to the docking results, the synthesized complexes exhibit promising features which enable them to be bound to the HIV-protease enzyme.

Automated summary

This study reports the synthesis and characterization of two new copper complexes, predicts their binding mode with HIV-1 protease through molecular docking, and reveals their stability and interactions through X-ray structural analysis and Hirshfeld surface analysis.