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机构地区:[1]玉林师范学院化学与生物系天然产物研究所,广西玉林市教育中路299号537000 [2]中南大学化学化工学院中草药现代化研究中心,长沙市410083 [3]中南大学湘雅医院药剂科,长沙市410008
出 处:《光谱实验室》2010年第1期49-54,共6页Chinese Journal of Spectroscopy Laboratory
基 金:国家自然科学基金重点项目(No20235020);教育部重点科技项目培育基金(No.704036);广西教育厅科研项目(No.200507217)
摘 要:荧光光谱、圆二色谱等多种光谱技术研究甲基莲心碱(NF)与人血清白蛋白(HSA)的相互作用,以Stern-Volmer和Lineweaver-Burk方程处理数据。甲基莲心碱对人血清白蛋白有较强的荧光猝灭作用并为静态猝灭,主要作用力为疏水作用和静电作用。309K下NF与HSA相互作用的结合常数为1.39×104L.mol-1,NF-色氨酸残基之间的距离为2.70nm,热力学参数ΔH0=-13.0KJ·mol-1,ΔS0=37.2J.(K.mol)-1。NF的结合使蛋白α-螺旋百分数增加。中药活性成分甘草次酸等和内源脂肪酸对结合的影响较少。With the help of multitude spectroscopic techniques, such as fluorescence spectra and circular dichroism, the interaction between neferinr (NF) and human serum albumin (HSA) was studied. Experimental datas were dealed with Stern-Volmer plot and Line weaver-Burk equation. The NF has a powerful ability to quench the albumin's fluorescence in a static mode and the main binding forces were hydrophobic interaction and electrostatic action. Under 309K, the binding constant was 1.39×10^4L · mol^-1. Distance between NF and tryptophan residue was 2. 70nm. Thermodynamic parameters were △H^0=-13.0kJ · mol^-1,△S^0=37. 2J · (K · mol)^-1. Binding of NF with HSA can increase the percentage of a-helix of HSA. There was little effect of bioactive components in traditional Chinese medicine (glycyrrhetinic acid etc) and fatty acids on the binding.
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