CAJ | 학술논문

应用荧光法研究了姜黄素钐配合物与牛血清白蛋白（BSA）的结合反应．根据配合物对BSA的荧光猝灭效应，利用变温试验，求得相互作用的结合常数、结合位点数及热力学参数，由此推测猝灭机理和结合力类型；依据Forster能量转移理论计算结合距离；并利用探针进行结合点定位；用同步荧光光谱确定配合物对牛血清白蛋白结构的影响．结果表明，姜黄素钐配合物对BSA的内源荧光猝灭主要以静态方式，同时发生非辐射能量转移；由△Hθ和△sθ〈0推测范德华力与氢键是主要结合力；配合物在BSA分子的SiteⅡ位结合，结合距离为2．4nm；配合物改变了BSA分子构像，对色氨酸残基影响更大．
응용형광법연구료강황소삼배합물여우혈청백단백（BSA）적결합반응．근거배합물대BSA적형광졸멸효응，이용변온시험，구득상호작용적결합상수、결합위점수급열역학삼수，유차추측졸멸궤리화결합력류형；의거Forster능량전이이론계산결합거리；병이용탐침진행결합점정위；용동보형광광보학정배합물대우혈청백단백결구적영향．결과표명，강황소삼배합물대BSA적내원형광졸멸주요이정태방식，동시발생비복사능량전이；유△Hθ화△sθ〈0추측범덕화력여경건시주요결합력；배합물재BSA분자적SiteⅡ위결합，결합거리위2．4nm；배합물개변료BSA분자구상，대색안산잔기영향경대．
The binding of curcumin-samarium coordination and bovine serum albumin（BSA） was investi- gated by fluorescence method. According to the fluorescence quenching effect of the complex-BSA, the variable-temperature experiments were finished, from which the binding constants, the number of binding sites and the values of thermodynamic parameters were obtained. The quenching mechanism and the type of binding force were inferred. With the theory of forster energy transfer the distance was calculated. The probe was used for positioning and the synchronous fluorescence spectroscopies were scanned to monitor the effect of the complex on BSA. The results showed that the complex quenched the intrinsic fluorescence of BSA mainly by a static process;meanwhile the non-radiative energy transfer occurred. △Hθ and △sθ〈0 , suggesting van der Waals forces and hydrogen bonding was the main binding force. The binding occurred in the Site II of BSA molecular and the distance was 2.4 nm. The conformation of BSA molecu- lar was modified by the complex,which had a greater effect on tryptophan residues.