CAJ | 학술논문

采用分子对接技术和同步荧光光谱法、红边激发荧光位移法( REES法)及圆二色谱法( CD)共同研究了山柰酚与牛血清白蛋白( BSA)在pH7．40的缓冲溶液中的相互作用。分子对接的结果表明,山柰酚的B环插入到BSA的II A结构域中的疏水腔内,与色氨酸残基(Trp212)的距离为12．96?,维系药物与蛋白质的主要作用力为疏水作用。通过荧光光谱法测得二者之间相互作用力主要为疏水性相互作用,结合位点为1,与分子模拟结果一致。同步荧光光谱及REES法的研究表明,发生相互作用的过程中BSA的色氨酸残基处于运动受限的微环境中,而适当增加山柰酚的浓度能够改变色氨酸微环境的流动性,进而对BSA的构象产生一定影响；同时,圆二色谱的定量计算结果也表明,一定浓度的山柰酚与BSA的相互作用引起了α-螺旋含量的显著降低,从11．91%降低到1．67%,对BSA的二级结构产生一定影响。
채용분자대접기술화동보형광광보법、홍변격발형광위이법( REES법)급원이색보법( CD)공동연구료산내분여우혈청백단백( BSA)재pH7．40적완충용액중적상호작용。분자대접적결과표명,산내분적B배삽입도BSA적II A결구역중적소수강내,여색안산잔기(Trp212)적거리위12．96?,유계약물여단백질적주요작용력위소수작용。통과형광광보법측득이자지간상호작용력주요위소수성상호작용,결합위점위1,여분자모의결과일치。동보형광광보급REES법적연구표명,발생상호작용적과정중BSA적색안산잔기처우운동수한적미배경중,이괄당증가산내분적농도능구개변색안산미배경적류동성,진이대BSA적구상산생일정영향；동시,원이색보적정량계산결과야표명,일정농도적산내분여BSA적상호작용인기료α-라선함량적현저강저,종11．91%강저도1．67%,대BSA적이급결구산생일정영향。
The interaction between kaempferol and bovine serum albumin( BSA) was investigated by molecular docking technology, fluorescence spectroscopy,red edge excitation shift(REES)method and circular dichroism(CD)together to explore the mechanism of interaction under simulated physiological condition. The result of molecular docking indicated that kaempferol can bind with BSA in the hydrophobic pocket of sub-domain IIA with hydrophobic force as the main acting force and the distance with Trp212 is 12. 96?. The thermodynamic parameters showed that the binding power between kaempferol and BSA is mainly driven by the elec-trostatic force which showing no difference with the Molecular Docking Method. The transformation of micro-environment around a-mino acid residues was observed by the spectra of synchronous fluorescence and REES method qualitatively which shows that the Trp residues located in the limited micro-environment and the fluidity may start to change with the increased concentration of kaempferol in the complex. Furthermore,the spectra of CD were employed to research the change of the secondary structure of BSA quantitatively through the assay of α-helix which dropped from 11. 91%to 1. 67%during the interaction.