化学研究与应用
化學研究與應用
화학연구여응용
CHEMICAL RESEARCH AND APPLICATION
2014年
10期
1551-1556
,共6页
苦参碱合Fe%人血清白蛋白%荧光光谱和紫外光谱法%圆二色谱法%荧光猝灭
苦參堿閤Fe%人血清白蛋白%熒光光譜和紫外光譜法%圓二色譜法%熒光猝滅
고삼감합Fe%인혈청백단백%형광광보화자외광보법%원이색보법%형광졸멸
matrine-Fe%human serum albumin(HSA)%fluorescence spectrometry and ultraviolet spectroscopy%circular dichroism
采用具有天然抗肿瘤活性的药物苦参碱为配体,与Fe( III)反应得到黄色的离子型苦参碱Fe( III)化合物[ H-Matrine][ FeCl4],用X射线单晶衍射分析法确定了配合物的结构,并在模拟生理条件下,利用紫外光谱法、荧光光谱法、同步荧光光谱和圆二色谱法研究了化合物[ H-Matrine][ FeCl4]与人血清白蛋白( HSA)的相互作用。结果表明：[ H-Matrine][ FeCl4]对 HSA的荧光产生猝灭作用,猝灭机制为静态猝灭；[ H-Matrine][ FeCl4]与HSA在不同温度下的结合常数K和结合位点数n,及其相关热力学参数ΔH、ΔG、ΔS,室温时分别为：1．03×106L·mol-1、1．24、-68．63KJ·mol、-34．30KJ·mol和114．05J·mol,且其相互作用力主要是静电作用力。同步荧光光谱的结果表明：[ H-Matrine][ FeCl4]与HSA的结合位点靠近色氨酸,并使色氨酸的疏水性减弱。
採用具有天然抗腫瘤活性的藥物苦參堿為配體,與Fe( III)反應得到黃色的離子型苦參堿Fe( III)化閤物[ H-Matrine][ FeCl4],用X射線單晶衍射分析法確定瞭配閤物的結構,併在模擬生理條件下,利用紫外光譜法、熒光光譜法、同步熒光光譜和圓二色譜法研究瞭化閤物[ H-Matrine][ FeCl4]與人血清白蛋白( HSA)的相互作用。結果錶明：[ H-Matrine][ FeCl4]對 HSA的熒光產生猝滅作用,猝滅機製為靜態猝滅；[ H-Matrine][ FeCl4]與HSA在不同溫度下的結閤常數K和結閤位點數n,及其相關熱力學參數ΔH、ΔG、ΔS,室溫時分彆為：1．03×106L·mol-1、1．24、-68．63KJ·mol、-34．30KJ·mol和114．05J·mol,且其相互作用力主要是靜電作用力。同步熒光光譜的結果錶明：[ H-Matrine][ FeCl4]與HSA的結閤位點靠近色氨痠,併使色氨痠的疏水性減弱。
채용구유천연항종류활성적약물고삼감위배체,여Fe( III)반응득도황색적리자형고삼감Fe( III)화합물[ H-Matrine][ FeCl4],용X사선단정연사분석법학정료배합물적결구,병재모의생리조건하,이용자외광보법、형광광보법、동보형광광보화원이색보법연구료화합물[ H-Matrine][ FeCl4]여인혈청백단백( HSA)적상호작용。결과표명：[ H-Matrine][ FeCl4]대 HSA적형광산생졸멸작용,졸멸궤제위정태졸멸；[ H-Matrine][ FeCl4]여HSA재불동온도하적결합상수K화결합위점수n,급기상관열역학삼수ΔH、ΔG、ΔS,실온시분별위：1．03×106L·mol-1、1．24、-68．63KJ·mol、-34．30KJ·mol화114．05J·mol,차기상호작용력주요시정전작용력。동보형광광보적결과표명：[ H-Matrine][ FeCl4]여HSA적결합위점고근색안산,병사색안산적소수성감약。
Matrine,a natural antitumor active a herbal plant,was selected as a 1igand to react with Fe(III)salt and to get a yellow [H-Matrine][FeCl4]ionic compound,which was characterized by single crystal X-ray diffraction analysis. The interactions of[H-Matrine][FeCl4]ionic compound with Human serum albumin(HSA)have investigated under the simulative human physiological conditions. The results of fluorescence spectrometry showed that the endogenous fluorescence of HSA has been significantly quenched by[ H-Matrine] [ FeCl4 ] and the mechanism of fluorescence quenching was static quenching. On the condition of room temperature(301K),the binding parameters and the thermodynamic parameters of[H-Matrine][FeCl4]and HSA are as follows:the binding constants is 1. 03×106L·mol-1,the numbers of binding sites is 1. 24,ΔH is-68. 63KJ·mol,ΔG is-34. 30KJ·mol andΔS is 114. 05J·mol,respectively. And the major driving force is Electrostatic interactions. The results of synchronous fluorescence demon-strated that the binding site of[ H-Matrine] [ FeCl4 ] and HSA is closer to tryptophan residues and the hydrophobicity of tryptophan residues was decrease.
