Probing the Binding of the Flavonoid Diosmetin to Human Serum Albumin by Multispectroscopic Techniques

• DOI: 10.1021/jf205260g
• Publication Date: 2012-02-22T02:15:46Z
• Authors: Guowen Zhang; Lin Wang; Junhui Pan
• Keywords: Human serum albumin; Binding constant

The binding mechanism of molecular interaction between diosmetin and human serum albumin (HSA) in a pH 7.4 phosphate buffer was studied using atomic force microscopy (AFM) various spectroscopic techniques including fluorescence, resonance light scattering (RLS), UV–vis absorption, circular dichroism (CD), Fourier transform infrared (FT–IR) spectroscopy. Fluorescence data revealed that the fluorescence quenching HSA by static procedure. constants number sites were evaluated at different temperatures. RLS spectra AFM images showed dimension individual molecules larger after with diosmetin. thermodynamic parameters, ΔH° ΔS° calculated to be −24.56 kJ mol–1 14.67 J K–1, respectively, suggesting diosmtin driven mainly hydrophobic interactions hydrogen bonds. displacement studies denaturation experiments presence urea indicated site I as main for on HSA. distance determined 3.54 nm based Förster theory. Analysis CD FT–IR demonstrated conformation slightly altered