高等学校化学学报
高等學校化學學報
고등학교화학학보
CHEMICAL JOURNAL OF CHINESE UNIVERSITIES
2015年
6期
1033-1041
,共9页
闻金燕%吕标彪%张阳%王家敏%应晓%王惠%计亮年%刘海洋
聞金燕%呂標彪%張暘%王傢敏%應曉%王惠%計亮年%劉海洋
문금연%려표표%장양%왕가민%응효%왕혜%계량년%류해양
咔咯%镓%人血清蛋白%相互作用
咔咯%鎵%人血清蛋白%相互作用
잡각%가%인혈청단백%상호작용
Corrole%Gallium%Human serum albumin%Interaction
利用紫外吸收光谱、荧光光谱、圆二色(CD)光谱和分子对接计算探究了5,10,15-三[4-(N-甲基-吡啶)]咔咯镓配合物(1-Ga)与人血清蛋白(HSA)的相互作用.结果表明, HSA的荧光能被1-Ga静态猝灭,两者的结合常数为2.82×104 L/mol,作用距离为3.342 nm.热力学参数显示1-Ga主要通过氢键和疏水作用与HSA结合,位点标记竞争实验表明1-Ga优先结合HSA的布洛芬位点Ⅱ.此外,紫外吸收光谱和CD光谱显示二者的相互作用会导致HSA α-螺旋结构的减少.分子对接计算结果表明1-Ga优先结合在HSA亚结构域ⅢA的位点Ⅱ疏水袋中.
利用紫外吸收光譜、熒光光譜、圓二色(CD)光譜和分子對接計算探究瞭5,10,15-三[4-(N-甲基-吡啶)]咔咯鎵配閤物(1-Ga)與人血清蛋白(HSA)的相互作用.結果錶明, HSA的熒光能被1-Ga靜態猝滅,兩者的結閤常數為2.82×104 L/mol,作用距離為3.342 nm.熱力學參數顯示1-Ga主要通過氫鍵和疏水作用與HSA結閤,位點標記競爭實驗錶明1-Ga優先結閤HSA的佈洛芬位點Ⅱ.此外,紫外吸收光譜和CD光譜顯示二者的相互作用會導緻HSA α-螺鏇結構的減少.分子對接計算結果錶明1-Ga優先結閤在HSA亞結構域ⅢA的位點Ⅱ疏水袋中.
이용자외흡수광보、형광광보、원이색(CD)광보화분자대접계산탐구료5,10,15-삼[4-(N-갑기-필정)]잡각가배합물(1-Ga)여인혈청단백(HSA)적상호작용.결과표명, HSA적형광능피1-Ga정태졸멸,량자적결합상수위2.82×104 L/mol,작용거리위3.342 nm.열역학삼수현시1-Ga주요통과경건화소수작용여HSA결합,위점표기경쟁실험표명1-Ga우선결합HSA적포락분위점Ⅱ.차외,자외흡수광보화CD광보현시이자적상호작용회도치HSA α-라선결구적감소.분자대접계산결과표명1-Ga우선결합재HSA아결구역ⅢA적위점Ⅱ소수대중.
The interaction between gallium 5 , 10 , 15-tris ( 4-methylpyridiniumyl ) corrole ( 1-Ga ) and human serum albumin( HSA) was investigated using UV-Vis spectra, fluorescence spectra, circular dichroism( CD) spectra and molecular docking simulation. The results reveal that the fluorescence quenching of HSA by 1-Ga is a static quenching process. The binding constant of complex 1-Ga with HSA is 2. 82×104 L/mol, and bin-ding distance r=3. 342 nm. Thermodynamic parameters show the interaction is mainly driven by hydrophobic and hydrogen binding forces. Site marker competition experiment indicates 1-Ga preferably bind to ibuprofen site Ⅱ of HSA. Also, α-helix content of HSA will decrease upon binding 1-Ga as indicated by UV-Vis and CD spectroscopy. Molecular docking simulation confirmed 1-Ga bind to the hydrophobic pocket site Ⅱ in domain ⅢA of HSA.