title: [Study on thermodynamics of binding reaction of dipyridamole with bovine serum albumin].
abstract: The binding feature of dipyridamole with bovine serum albumin (BSA) was studied using fluorescence spectroscopy. It was shown that this compound has a powerful ability to quench the BSA fluorescence via a nonradiative energy transfer mechanism. The fluorescence quenching data were analyzed according to stern-volmer equation and double-reciprocal equation, and the binding constant and the thermodynamic parameters were obtained.
authors.affiliation: Department of Chemistry, Jinzhou Normal University, Jinzhou 434020, China.
authors.forename: Cheng-nong
authors.initials: CN
authors.lastname: Yan
authors.forename: Yun-feng
authors.initials: YF
authors.lastname: Shangguan
authors.forename: Jin-qiang
authors.initials: JQ
authors.lastname: Tong
authors.forename: Yi
authors.initials: Y
authors.lastname: Liu
authors.forename: Dai-wen
authors.initials: DW
authors.lastname: Pang
authors.forename: Zu-ting
authors.initials: ZT
authors.lastname: Pan
authors.forename: Song-sheng
authors.initials: SS
authors.lastname: Qu
mesh_terms: D000818:Animals; D002417:Cattle; D004176:Dipyridamole / Q000737:chemistry*; D004735:Energy Transfer; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics; D014665:Vasodilator Agents / Q000737:chemistry
chemical_list: D014665:Vasodilator Agents; D012710:Serum Albumin, Bovine; D004176:Dipyridamole