title: Study on the interaction between salvianic acid A sodium and bovine serum albumin by spectroscopic methods.
abstract: The interaction between salvianic acid A sodium (SAS) and bovine serum albumin (BSA) was investigated using fluorescence and ultraviolet spectroscopy at different temperatures under imitated physiological conditions. The experimental results showed that the fluorescence of BSA was quenched by SAS through a static quenching procedure. The binding constants of SAS with BSA were 2.03, 1.17 and 0.71×10(5) L mol(-1) at 291, 298 and 305 K, respectively. Negative values of ΔG, ΔH, and ΔS indicate that the interaction between SAS and BSA is driven by hydrogen bonds and van der Waals forces. According to Förster non-radiation energy transfer theory, the binding distance between BSA and SAS was calculated to be about 2.92 nm. The effect of SAS on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy. In addition, the effect of some metal ions Cu(2+), Ca(2+), Mg(2+), and Zn(2+) on the binding constant between SAS and BSA was examined.
authors.affiliation: Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of Education, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan, China.
authors.forename: Ronghua
authors.initials: R
authors.lastname: Liu
authors.forename: Xianyong
authors.initials: X
authors.lastname: Yu
authors.forename: Wei
authors.initials: W
authors.lastname: Gao
authors.forename: Danhong
authors.initials: D
authors.lastname: Ji
authors.forename: Fengxian
authors.initials: F
authors.lastname: Yang
authors.forename: Xiaofang
authors.initials: X
authors.lastname: Li
authors.forename: Jian
authors.initials: J
authors.lastname: Chen
authors.forename: Hongwen
authors.initials: H
authors.lastname: Tao
authors.forename: Haowen
authors.initials: H
authors.lastname: Huang
authors.forename: Pinggui
authors.initials: P
authors.lastname: Yi
mesh_terms: D000143:Acids / Q000737:chemistry*; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004735:Energy Transfer; D007477:Ions; D007700:Kinetics; D007773:Lactates / Q000737:chemistry*; D008670:Metals / Q000737:chemistry; D008968:Molecular Conformation; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics
chemical_list: D000143:Acids; D007477:Ions; D007773:Lactates; D008670:Metals; D012710:Serum Albumin, Bovine; C035055:3,4-dihydroxyphenyllactic acid