光谱学与光谱分析
光譜學與光譜分析
광보학여광보분석
SPECTROSCOPY AND SPECTRAL ANALYSIS
2009年
12期
3369-3374
,共6页
刘蓉%曹树稳%余燕影%李先和%邓泽元
劉蓉%曹樹穩%餘燕影%李先和%鄧澤元
류용%조수은%여연영%리선화%산택원
染料木素%酯化修饰物%牛血清白蛋白%荧光光谱法
染料木素%酯化脩飾物%牛血清白蛋白%熒光光譜法
염료목소%지화수식물%우혈청백단백%형광광보법
Genistein%Esterified derivatives%Bovine serum albumin(BSA)%Fluorescence spectroscopy
在模拟人体生理条件下(pH=7.4),利用荧光光谱和紫外分光光度法研究了染料木素7-乙酰阿魏酸酯(1)和染料木素7,4'-二-乙酰阿魏酸酯(2)两种新型染料木素酯化修饰物,与牛血清白蛋白(BSA)的相互作用.实验表明:两种染料木素阿魏酸酯均能有效猝灭BSA的内源荧光,低浓度时为静态猝灭过程.考察了不同温度下化合物与BSA的结合常数和结合位点数.根据反应热力学参数确定了BSA与1之间主要为静电力作用,与2之间主要为氢键和范德华力作用.根据Forster非辐射能量转移理论,BSA(给体)与化合物(受体)间的结合距离r分别为2.63和2.92 nm.同步荧光光谱法研究表明,染料木素乙酰阿魏酸酯与BSA的结合不影响蛋白质的构象,结合位点更接近于色氨酸.
在模擬人體生理條件下(pH=7.4),利用熒光光譜和紫外分光光度法研究瞭染料木素7-乙酰阿魏痠酯(1)和染料木素7,4'-二-乙酰阿魏痠酯(2)兩種新型染料木素酯化脩飾物,與牛血清白蛋白(BSA)的相互作用.實驗錶明:兩種染料木素阿魏痠酯均能有效猝滅BSA的內源熒光,低濃度時為靜態猝滅過程.攷察瞭不同溫度下化閤物與BSA的結閤常數和結閤位點數.根據反應熱力學參數確定瞭BSA與1之間主要為靜電力作用,與2之間主要為氫鍵和範德華力作用.根據Forster非輻射能量轉移理論,BSA(給體)與化閤物(受體)間的結閤距離r分彆為2.63和2.92 nm.同步熒光光譜法研究錶明,染料木素乙酰阿魏痠酯與BSA的結閤不影響蛋白質的構象,結閤位點更接近于色氨痠.
재모의인체생리조건하(pH=7.4),이용형광광보화자외분광광도법연구료염료목소7-을선아위산지(1)화염료목소7,4'-이-을선아위산지(2)량충신형염료목소지화수식물,여우혈청백단백(BSA)적상호작용.실험표명:량충염료목소아위산지균능유효졸멸BSA적내원형광,저농도시위정태졸멸과정.고찰료불동온도하화합물여BSA적결합상수화결합위점수.근거반응열역학삼수학정료BSA여1지간주요위정전력작용,여2지간주요위경건화범덕화력작용.근거Forster비복사능량전이이론,BSA(급체)여화합물(수체)간적결합거리r분별위2.63화2.92 nm.동보형광광보법연구표명,염료목소을선아위산지여BSA적결합불영향단백질적구상,결합위점경접근우색안산.
Under the imitated physiological conditions(pH=7.4), the interactions of two novel genistein esterified derivatives, genistein 7-acetylferulic acid ester and genistein 7, 4'-di-acetylferulic acid ester(1 and 2), with bovine serum albumin (BSA) were investigated by the fluorescence and UV-Vis spectroscopy. It was observed that both of them can effectively quench the in-trinsic fluorescence of BSA. The results suggested that the fluorescence quenching process of BSA at low concentrations of the compounds may be mainly governed by static quenching mechanisms. The binding constants (K_A) and the number of binding sites (n) at different temperatures were calculated. From the thermodynamic parameters, it can be judged that the binding of 1 to BSA involved electrostatic interactions, whereas the binding of 2 to BSA involved hydrogen bonds and Van der Waals forces. The binding average distances r between BSA( donor) and the compounds (acceptor) were determined to be 2. 63 nm and 2. 92 nm respectively based on the F6rster theory. Besides, the interactions of BSA with the compounds did not change the conformationof BSA and the binding of compounds to BSA is near tryptophan subunit via synchronous fluorescence spectrometry.