摘要
本文用荧光光谱法、分光光度法研究了水溶液中喹诺酮类药物司帕沙星与牛血清白蛋白 (BSA)、鸡蛋白 (CEA)的相互作用 ,求得它们间的结合常数为K鸡 =8 2 9× 10 6,K牛 =4 41× 10 7;结合位点数分别为n鸡=0 5 88,n牛 =0 793,并根据F rster非辐射能量转移机制 ,测定了司帕沙星与两种血清白蛋白相互结合时其给体 受体间距离 (R鸡 =1 99nm ,R牛 =2 0 9nm)和能量转移效率 (E鸡 =0 76 6 ,E牛 =0 714)。实验表明 ,随着温度升高 ,BSA及CEA的猝灭曲线斜率降低 ,证实了司帕沙星与BSA和CEA的相互结合作用为单一的静态猝灭过程 ,其作用机制属能量转移机制。通过两种血清白蛋白与抗菌药物司帕沙星结合反应 ,探讨了药物司帕沙星在生物体内与蛋白质的相互作用的生物学效应及其作用机理。
The binding reaction between sparfloxacion (SPFX) and bovine serum albumin (BSA) or chicken egg albumin (CEA) in aqueous was studied using fluorescence and absorption spectra. Their binding constants are K-CEA = 8.29 X 10(6) and K-BSA = 4.41 X 10(7), and the binding sites are n(CEA) = 0.558, n(BSA) = 0.793 respectively. The action distances (R-CEA = 1. 99 nm, R-BSA = 2.09 nm) and energy transfer efficiencies (E-CEA = 0. 766, E-BSA = 0. 714) between donor-acceptor and SPFX were obtained by Forster's nonradiative energy transfer mechanism. The experiment demonstrated that the higher the temperature is, the lower the slopes of quenching curves of BSA and CEA are in presence of different amounts of SPFX. It is confirmed that the combination for SPFX with BSA or CEA is a single static quenching process, their interaction may be interpreted with energy transfer mechanism. Through binding reaction of the two albumins with SPFX, the biological effects and action mechanism of SPFX with albumins in vivo were discussed.
出处
《光谱学与光谱分析》
SCIE
EI
CAS
CSCD
北大核心
2001年第6期829-832,共4页
Spectroscopy and Spectral Analysis
基金
博士点基金
国家自然科学基金资助课题
