Fluorometric investigation of the interaction of bovine serum albumin with surfactants and 6-mercaptopurine.
Fluorescence quenching in solutions of bovine serum albumin has been investigated in the presence of 6-mercaptopurine and ionic surfactants. Spectroscopic analysis of the emission quenching at different temperatures revealed that the quenching mechanism of bovine serum albumin by 6-mercaptopurine was dynamic quenching mechanism. The Stern-Volmer quenching model has been successfully applied, and the activation energy of the interaction between 6-mercaptopurine and bovine serum albumin as much as 4.26 kJ mol(-1) was calculated. The distance r between donor (bovine serum albumin) and acceptor (6-mercaptopurine) was obtained according to fluorescence resonance energy transfer (FRET). The result of synchronous fluorescence spectra shows that the conformation of bovine serum albumin has been changed at the present of 6-mercaptopurine.
Hu
Yan-Jun
YJ
Department of Chemistry, College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China.
Liu
Yi
Y
Jiang
Wei
W
Zhao
Ru-Ming
RM
Qu
Song-Sheng
SS
D000077286:Cetrimonium; D002593:Cetrimonium Compounds; D007202:Indicators and Reagents; D015122:Mercaptopurine; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence / Q000379:methods; D013501:Surface-Active Agents
D002593:Cetrimonium Compounds; D007202:Indicators and Reagents; D013501:Surface-Active Agents; D012710:Serum Albumin, Bovine; D015122:Mercaptopurine; D000077286:Cetrimonium