【摘要】 应用荧光光谱法及紫外可见光谱的方法研究了氨曲南与牛血清白蛋白(BSA)的相互作用。实验结果表明,氨曲南能强烈猝灭牛血清白蛋白的荧光强度,其荧光猝灭机理为动态猝灭。在此基础上计算了二者相互作用的结合常数、结合位点数及ΔH、ΔG、ΔS等热力学参数等。结果表明氨曲南与BSA以1∶1结合,其反应为熵驱动,相互作用力主要为疏水力。根据Frster无辐射能量转移理论计算了给体(BSA)和受体(氨曲南)之间的结合距离,并用同步荧光技术考察了氨曲南对牛血清白蛋白构象的影响。更多还原

【Abstract】 The interaction between aztreonam and bovine serum albumin(BSA)was studied by fluorescence spectroscopy and UV-vis absorption spectroscopy.Experimental results showed that the fluorescence intensity of BSA was quenched strongly by aztreonam due to the formation of an aztreonam-BSA complex.The mechanism is a static quenching procedure.The number of binding sites n and apparent binding constant Kb were measured by fluorescence quenching method.The corresponding thermodynamics parameters ΔH、ΔG、ΔS were calculated.The results indicated aztreonam and BSA were combined with the ratio of 1∶1,the reaction was driven by entropy and the interaction force was mostly hydrophobic force.The distance between the donor(BSA)and the acceptor(Aztreonam) was obtained according to Frster theory of non-radiation energy transfer,and effect of bovine serum aztreonam on protein conformation was studied with synchronous fluorescence technique.更多还原