Human serum albumin interaction studies of a new copper(II) complex containing ceftobiprole drug using molecular modeling and multispectroscopic methods

Abstract

A copper(II) complex containing the ceftobiprole drug and 1,10-phenanthroline (phen) has been synthesized and characterized by UV–vis, FT-IR and mass spectra, and elemental analysis. The binding interaction between [Cu(cef)(phen)Cl₂] complex and human serum albumin (HSA) was investigated using absorption, fluorescence emission and circular dichroism spectroscopies, and molecular docking. Thermodynamic parameters (ΔH < 0 and ΔS < 0) indicated that the hydrogen bond and van der Waals interactions played main roles in the binding of complex [Cu(cef)(phen)Cl₂] to HSA. The results of CD and UV–vis spectroscopy showed that the binding of [Cu(cef)(phen)Cl₂] to HSA induces some conformational changes in HSA. Displacement experiments predicted that the binding of [Cu(cef)(phen)Cl₂] complex to HSA is located within domain III, Sudlow’s site 2, and these observations were substantiated by molecular docking studies.

Keywords:

• [Cu(cef)(phen)Cl₂] complex
• HSA
• molecular modeling
• fluorescence quenching
• ceftobiprole drug