Study of the Binding of Cuminaldehyde with Bovine Serum Albumin by Spectroscopic and Molecular Modeling Methods

Here, we investigated the interaction of cuminaldehyde with a model carrier protein, bovine serum albumin (BSA). The formation BSA–cuminaldehyde complex was confirmed through ultraviolet–visible (UV–Vis) spectroscopy and further proven by detailed intrinsic fluorescence spectroscopic measurements. As observed, quenched tryptophanyl BSA. data, before analyses, were corrected for inner filter effect (IFE) because significant absorption at excitation wavelength that employed in typical Stern–Volmer plots slightly nonlinear; they exhibited negative deviation toward x-axis, phenomenon is observed proteins possessing more than one tryptophan residue. Thus, modified equation to analyze data. analyzed data revealed BSA proceeded via static quenching mechanism there fair 1 : binding between them. strengthened hydrophobic forces hydrogen bonding. A lowered concentration did not affect secondary structure BSA, although an increased partially exposed protein decreasing its ?-helical contents. molecular dockings simulations stable complex. silico results also contributions bonding driving imparted stability.