作者: Di Yao , Shouhai Ni , Maogui Wen , Hedong Bian , Qing Yu
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摘要: Fluorescence spectroscopy, Fourier transform infrared (FT-IR) circular dichroism (CD) and FT-Raman spectroscopy were employed to analyze the binding of asiatic acid (AA) bovine serum albumin (BSA) under simulative physiological conditions. data revealed that fluorescence quenching BSA by AA was result formation BSA-AA complex. The mechanism a static procedure. According Van′t Hoff equation, thermodynamic parameters enthalpy change (ΔH0) entropy (ΔS0) for reaction evaluated be −12.55 kJ·mol−1 67.08 kJ·mol−1, respectively, indicating hydrophobic electrostatic interactions played major role in stabilizing influence on conformation has also been analyzed basis FT-IR, CD spectra.