title: 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 310 K) were 1.82, 2.69, and 3.4 × 10(4)L mol(-1), respectively. The distance between donor (BSA) and acceptor (MH) was 5.54 nm 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.
authors.affiliation: School of Materials and Chemical Engineering, Xi'an Technological University, Xi'an 710032, China. lijhua09@163.com
authors.forename: Jinhua
authors.initials: J
authors.lastname: Li
authors.forename: Sumin
authors.initials: S
authors.lastname: Wang
mesh_terms: D000818:Animals; D002417:Cattle; D006569:Hesperidin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D017550:Spectroscopy, Fourier Transform Infrared; D013816:Thermodynamics
chemical_list: D012710:Serum Albumin, Bovine; D006569:Hesperidin; C052037:methyl hesperidin