A study on the interaction between 3‐spiro‐piperidones and bovine serum albumin using spectroscopic approaches

Abstract

The interaction between 3-spiro-2'-pyrrolidine-3'-spiro-3″-piperidine-2,3″-dione (PPD) and bovine serum albumin (BSA) in aqueous solution was studied using fluorescence and UV-vis spectroscopy. Fluorescence emission data revealed that BSA (1.00 × 10(-5) mol/L) fluorescence was statically quenched by PPD at various concentrations, which implies that a PPD-BSA complex was formed. The binding constant (KA ), the number of binding sites (n) and the specific binding site of the PPD with BSA were determined. Energy-transfer efficiency parameters were determined and the mechanism of the interaction discussed. The thermodynamic parameters, ΔG, ΔH and ΔS, were obtained according to van't Hoff's equation, showing the involvement of hydrophobic forces in these interactions. The effect of PPD acting on the BSA conformation was detected by synchronous fluorescence.

Using resonance light scattering and UV/vis absorption spectroscopy to study the interaction between gliclazide and bovine serum albumin

“…When an excitation wavelength at 280 nm is adopted, BSA naturally fluoresces at 340 nm, and this fluorescence is mainly attributed to emission by tryptophan and tyrosine residues . The fluorescence spectra of BSA in the presence of gliclazide at different concentrations and 298 K are shown in Fig.…”