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.
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