title: Characterization of the interaction between reserpine and bovine serum albumin: spectroscopic approaches.
abstract: The characteristics of the interaction between reserpine and bovine serum albumin (BSA) were studied by fluorescence, UV-vis absorption and Fourier transform infrared (FT-IR) spectroscopy. Spectroscopic analysis revealed that fluorescence quenching of BSA by reserpine was through a static quenching procedure. The binding constant K(A) of reserpine with BSA at 293, 301 and 309 K was 1.63, 1.78 and 2.35 x 10(5) moL(-1) L respectively, which indicated degree of binding force between reserpine and BSA. There was one binding site between reserpine and BSA. The entropy and enthalpy changes were positive, indicating that interaction of reserpine and BSA was driven mainly by hydrophobic forces. The average binding distance between the donor (BSA) and the acceptor (reserpine) was about 3.84 nm based on the Forster non-radiation energy transfer theory. Results of synchronous fluorescence and FT-IR spectra indicated that the conformation and microenvironment of BSA were changed by the binding of reserpine. The results may provide important insights into the physiological activity of reserpine.
authors.affiliation: College of Science, Nanjing University of Aeronautics and Astronautics, Nanjing City, Jiangsu Province 210016, P.R. China.
authors.forename: Tianhu
authors.initials: T
authors.lastname: Wang
authors.forename: Zhimin
authors.initials: Z
authors.lastname: Zhao
authors.forename: Jin
authors.initials: J
authors.lastname: Hua
authors.forename: Jihua
authors.initials: J
authors.lastname: Zhang
mesh_terms: D000818:Animals; D002417:Cattle; D012110:Reserpine / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D012710:Serum Albumin, Bovine; D012110:Reserpine