Probing the interaction of uranyl(VI) complex with bovine serum albumin via in-depth experimental and computational perspectives

Interaction aspects of uranyl(VI) complexes as well as the coordinated ONNO-donor ligand with bovine serum albumin (BSA) were investigated by the fluorescence spectroscopy and computational insights. Under optimal physiological condition, it was observed that there was significant decrease in fluorescence intensity of BSA upon interaction with uranyl(VI) complexes as well as the ligand. The mechanism of interaction between the uranyl (VI) complex and BSA protein was examined by fluorescence measurement. The Stern-Volmer constant, binding affinity, binding constant, standard free energy, and fluorescence lifetime decay profile of BSA in the absence as well as in the presence of uranyl(VI) complex were determined. Furthermore, the conformational binding of uranyl(VI) complexes with BSA protein was explored via molecular docking studies, and confirmed that there is a strong affinity between the Trp-213 residue in the binding pocket of sub-domain IIA and uranyl(VI) complex.

Automated summary

The interaction aspects of uranyl(VI) complexes and the ONNO-donor ligand with bovine serum albumin (BSA) were investigated using fluorescence spectroscopy and computational insights. It was observed that under optimal physiological conditions, the fluorescence intensity of BSA significantly decreased upon interaction with both the uranyl(VI) complexes and the ligand. The mechanism of interaction between the uranyl(VI) complex and BSA was examined, and various parameters such as binding affinity and fluorescence lifetime decay profile were determined.