化学研究与应用
化學研究與應用
화학연구여응용
CHEMICAL RESEARCH AND APPLICATION
2014年
7期
1048-1052
,共5页
邹雪晴%周雄威%邹婷%张业中%戴捷
鄒雪晴%週雄威%鄒婷%張業中%戴捷
추설청%주웅위%추정%장업중%대첩
二苯甲酮%人血清白蛋白%荧光光谱%位点竞争%三维荧光光谱
二苯甲酮%人血清白蛋白%熒光光譜%位點競爭%三維熒光光譜
이분갑동%인혈청백단백%형광광보%위점경쟁%삼유형광광보
benzophenone%human serum albumin%fluorescence spectroscopy%site marker competitive experiment%three-dimensional fluorescence spectra
在模拟人体生理条件下(pH=7.4),采用荧光光谱、位点竞争、三维荧光光谱研究了二苯甲酮(BP)与人血清白蛋白( HSA)之间的相互作用。根据修正的Stern-Volmer方程计算了不同温度下的结合常数,并结合Van’t Hoff方程计算出相应的热力学参数。实验结果表明,BP对HSA的猝灭机制为静态猝灭过程,氢键和范德华力是维持BP-HSA复合物稳定的主要作用力;位点竞争实验揭示了BP在HSA上的结合位点位于亚域结构II A上的疏水腔中( site I位);三维荧光光谱分析表明BP使HSA发生了轻微地解旋,HSA的二级结构发生了改变。
在模擬人體生理條件下(pH=7.4),採用熒光光譜、位點競爭、三維熒光光譜研究瞭二苯甲酮(BP)與人血清白蛋白( HSA)之間的相互作用。根據脩正的Stern-Volmer方程計算瞭不同溫度下的結閤常數,併結閤Van’t Hoff方程計算齣相應的熱力學參數。實驗結果錶明,BP對HSA的猝滅機製為靜態猝滅過程,氫鍵和範德華力是維持BP-HSA複閤物穩定的主要作用力;位點競爭實驗揭示瞭BP在HSA上的結閤位點位于亞域結構II A上的疏水腔中( site I位);三維熒光光譜分析錶明BP使HSA髮生瞭輕微地解鏇,HSA的二級結構髮生瞭改變。
재모의인체생리조건하(pH=7.4),채용형광광보、위점경쟁、삼유형광광보연구료이분갑동(BP)여인혈청백단백( HSA)지간적상호작용。근거수정적Stern-Volmer방정계산료불동온도하적결합상수,병결합Van’t Hoff방정계산출상응적열역학삼수。실험결과표명,BP대HSA적졸멸궤제위정태졸멸과정,경건화범덕화력시유지BP-HSA복합물은정적주요작용력;위점경쟁실험게시료BP재HSA상적결합위점위우아역결구II A상적소수강중( site I위);삼유형광광보분석표명BP사HSA발생료경미지해선,HSA적이급결구발생료개변。
The interaction between Benzophenone and human serum albumin was studied by the methods of fluorescence spectrosco-py combined with site marker competitive experiment and three-dimensional fluorescence spectra under the simulative physiological conditions. The corresponding association contants ( Ka ) at different temperatures have been determined by the modified Stern-Volmer equation,and the thermodynamic parameters were obtained by Van’ t Hoff equation. The experimental results indicated that the quenching mechanism of BP-HSA is a static process and the hydrogen bond and van der Waals played a great role in forming a stable complex. Site marker competitive experiments revealed that the binding site of BP to HSA located in sub-domainIIA( siteⅠ) . The change in the secondary structure of the protein was evident according to three dimensional fluorescence spectra,which showed that the presence of BP caused the slight looseness of the polypeptide of protein.