[Study on thermodynamics of binding reaction of dipyridamole with bovine serum albumin].
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.
Yan
Cheng-nong
CN
Department of Chemistry, Jinzhou Normal University, Jinzhou 434020, China.
Shangguan
Yun-feng
YF
Tong
Jin-qiang
JQ
Liu
Yi
Y
Pang
Dai-wen
DW
Pan
Zu-ting
ZT
Qu
Song-sheng
SS
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
D014665:Vasodilator Agents; D012710:Serum Albumin, Bovine; D004176:Dipyridamole