摘要
应用荧光光谱法和紫外可见吸收光谱法研究了在pH值7.4的Tris-HCl缓冲溶液中吡罗红B(PB)与牛血清白蛋白(BSA)相互作用的机制。结果表明,PB对BSA产生了荧光猝灭作用,且属于静态猝灭过程。计算得到298 K和308 K下的结合常数分别为7.1105×105L.mol-1和5.2614×105L.mol-1,结合位点数分别为1.2312和1.2057。热力学参数表明PB与BSA之间的相互作用力类型为静电作用力。用同步荧光法探讨了PB对BSA构象的影响。根据F rster非辐射能量转移理论计算出供体与受体间的结合距离r为1.98 nm,能量转移效率E为0.0393。
The interaction between pyronine B（PB）and bovine serum albumin（BSA）was studied under the conditions（pH value 7.4）of Tris-HCl buffer by fluorescence spectrometry and UV-visible absorption spectroscopy.The research showed that the interaction,which resulted in the fluorescence quenching of BSA,belonged to a static quenching mechanism.And by calculation the binding constants were 7.1105×105 L·mol-1（298 K）and 5.2614×105 L·mol-1（308 K）,and the binding sites were 1.2312（298 K）and 1.2057（308 K）.The thermodynamic parameters showed that the interaction between PB and BSA was mainly driven by electrostatic force.Synchronous fluorescence spectrum was used to investigate the conformational change of BSA.The shortest binding distance（r= 1.98 nm）and energy transfer efficiency（E= 0.0393）between donor（BSA） and acceptor（PB）were obtained by Frster′ s nonradiative energy transfer mechanism.
出处
《化学与生物工程》
CAS
2010年第11期59-62,共4页
Chemistry & Bioengineering
基金
安徽省高校自然科学基金资助项目(KJ2008A123)
关键词
吡罗红B
牛血清白蛋白
相互作用
荧光光谱
pyronine B
bovine serum albumin
interaction
fluorescence spectrometry
