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ABSTRACT
The aim of the present study is to investigate the urea-induced denaturation of bovine serum albumin. The native and denatured bovine serum albumin interactions with 32π-Norcorrole were investigated, respectively. The circular dichroism spectra indicated that the α-helix content of bovine serum albumin reduces in the presence of urea and 32π-Norcorrole. The Stern–Volmer quenching constant indicated that both dynamic and static quenching exist in the interaction; moreover, the denaturation of bovine serum albumin leads to the decrease of Stern–Volmer quenching constant. Binding constant illustrated that the native bovine serum albumin has stronger combination capacity than the denatured bovine serum albumin. The fluorescence lifetime studies demonstrated that denaturation lead to the fluorescence decay of bovine serum albumin. The binding sites experiment and molecular docking studies demonstrated that the binding site of 32π-Norcorrole on bovine serum albumin is mainly located in site I.