title: Study of the interaction between 2,5-di-[2-(4-hydroxy-phenyl)ethylene]-terephthalonitril and bovine serum albumin by fluorescence spectroscopy.
abstract: A new compound, 2,5-di-[2-(4-hydroxy-phenyl)ethylene]-terephthalonitrile (DHPEPN), was synthesized. The interaction between bovine serum albumin (BSA) and DHPEPN in Tris-HCl buffer solution (pH 7.4) was investigated using fluorescence and UV-vis absorption spectroscopy. The mechanism of BSA fluorescence quenched by DHPEPN is discussed according to the Stern-Volmer equation. The binding constant and the thermodynamic parameters ΔH, ΔS, ΔG at different temperatures were calculated. The results indicate that the van der Waals interaction and hydrogen bonding play major roles in the binding process. The distance between BSA and DHPEPN is estimated to be 3.59 nm based on the Förster resonance energy transfer theory. The spectral changes of synchronous fluorescence and three-dimensional fluorescence suggest that both of the microenvironment of DHPEPN and the conformation of BSA are changed during binding between DHPEPN and BSA.
authors: Department of Chemistry/Center of Analysis and Testing, Nanchang University, Nanchang, China.
authors: Li-Na
authors: LN
authors: Zhang
authors: Fang-Ying
authors: FY
authors: Wu
authors: Ai-Hong
authors: AH
authors: Liu
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004735:Energy Transfer; D007700:Kinetics; D009570:Nitriles / Q000737:chemistry / Q000378:metabolism*; D010795:Phthalic Acids / Q000737:chemistry / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D012997:Solvents; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics; D017186:Titrimetry
chemical_list: C560239:2,5-di-(2-(4-hydroxy-phenyl)ethylene)-terephthalonitril; D009570:Nitriles; D010795:Phthalic Acids; D012997:Solvents; D012710:Serum Albumin, Bovine; C011363:terephthalic acid