Combined voltammetric and spectroscopic analysis of small molecule-biopolymer interactions: the levodopa and serum albumin system.
Combined voltammetric and spectroscopic analysis of small molecule-biopolymer interactions: the levodopa and serum albumin system.
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DOI：
10.1016/j.talanta.2011.11.027
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发表时间：
2012-01
期刊：
影响因子：
6.1
通讯作者：
Qiulan Zhang;Y. Ni;S. Kokot
中科院分区：
文献类型：
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作者：
Qiulan Zhang;Y. Ni;S. Kokot
研究了一种同时测定左旋多巴（LD）等重要小分子与牛血清白蛋白（BSA）等生物大分子结合过程中反应物和产物的分析方法。伏安法和荧光光谱法被用来从不同的反应物混合物作为浓度的函数，以获得分析配置文件。这使得提取的平衡常数（KSV），这是第一次报道。伏安法结果支持LD-BSA复合物的形成，但不是与多巴胺。无法获得LD-BSA系统的更多信息，因为无法提取测量的复合物曲线。通过MCR-ALS方法对扩展数据矩阵进行解析，获得了新的信息。先前不可用的LD-BSA复合物的提取伏安图曲线表明复合物是电活性的;如果LD-BSA系统处于其折叠状态，这是出乎意料的，因此，建议蛋白质必须是解折叠的。药物：BSA化学计量比为3：1（即（左旋多巴）3-BSA）的观察结果支持这一建议;这些结果来自三种反应组分的MCR-ALS提取浓度曲线。
An analytical method was researched for the simultaneous determination of reactants and products during the binding of important small molecules such as levodopa (LD) with biopolymers such as bovine serum albumin (BSA). Voltammetry and fluorescence spectroscopy were used to obtain the analytical profiles from different reactant mixtures as a function of concentration. This enabled the extraction of the equilibrium constants (KSV) which are reported for the first time. Voltammetric results supported the formation of the LD–BSA complex but not that with dopamine. Further information of the LD–BSA system was unattainable because the measured composite profiles could not be extracted. New information was obtained when the extended data matrix was resolved by the MCR–ALS method. The previously unavailable extracted voltammogram profile of LD–BSA complex indicated that the complex was electroactive; this was unexpected if the LD–BSA system was in its folded state, and hence, it was suggested that the protein must be unfolded. The observation that the drug:BSA stoichiometry was 3:1, i.e. (levodopa)3–BSA, supported this suggestion; these results were obtained from the MCR–ALS extracted concentration profiles for the three reaction components.