Molecular spectroscopic on interaction between Methyl hesperidin and Buman serum albumin

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 310 K) were 1.82, 2.69, and 3.4 x 10(4) L mol(-1), respectively. The distance between donor (BSA) and acceptor (MH) was 5.54 nm according to the Forster 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. 2012 Elsevier B.V. All rights reserved.