Molecular spectroscopic on interaction between Methyl hesperidin and Buman serum albumin

Abstract: The interaction of Methyl hesperidin (MH) with Buman serum albumin was studied by spectroscopic methods including Fluorescence quenching technology, UV absorbance spectra and Fourier transform infrared (FT-IR) spectroscopy under simulative physiological conditions. The result of fluorescence titration revealed that Methyl hesperidin could quench the intrinsic fluorescence of BSA and the quenching mechanism should be a combined quenching process. The binding constants at three temperatures (296, 303, and 310K) were 1.82, 2.69, and 3.4×104 Lmol−1, respectively. The distance between donor (BSA) and acceptor (MH) was 5.54nm according to the Förster theory of non-radiation energy transfer. In addition, FT-IR spectroscopy showed that the binding of MH to BSA changed the secondary structure of protein. [Copyright &y& Elsevier]