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Spectrophotometer measurements to characterize conformational state of the proteins: p53 analysis

机译：分光光度计测量以表征蛋白质的构象状态：p53分析

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The development of sensing techniques for the analysis of protein samples represents an area of great interest for biotechnology, pharmacology and diagnostics. Traditional biochemical assays available present limitations in term time and cost efficiency. On the contrary, optical based techniques, such as spectrophotometry, might offer the interesting possibility of a non-invasive and continuous monitoring. The present work proposes a spectrophotometer-based method of identifying different conformational states of p53, a redox sensitive protein involved in several pathophysiological processes. Samples containing three different structural states of p53 (Wild type p53, Denatured p53 and Oxidized p53) has been investigated using spectrophotometer in a measuring wavelength range from 185nm to 1400nm, in order to detect the differences in light absorption. The unfolding state of p53 redox products has been further studied performing a label-based silver stripping voltammetry. Results from the spectrophotometric analysis showed different absorbance peaks at distinct wavelength for each conformation, suggesting the possibility to use this technique to discriminate the different p53 redox products tested. Further, these results appeared to be well supported from the binding-affinity label-based test. Overall the study allowed to state the possibility to identify p53 different conformational states through this simple and non-invasive method, thus reducing the complexity of the procedures involved in conventional methods.
机译：用于蛋白质样品分析的传感技术的发展代表了对生物技术，药理学和诊断学的极大兴趣。可用的传统生化测定法在时间和成本效率方面存在局限性。相反，基于光学的技术（例如分光光度法）可能会提供有趣的无创且连续监测的可能性。本工作提出了一种基于分光光度计的方法来鉴定p53的不同构象状态，p53是一种参与多种病理生理过程的氧化还原敏感蛋白。为了检测光吸收的差异，已使用分光光度计在185nm至1400nm的测量波长范围内研究了包含p53三种不同结构状态（野生型p53，变性p53和氧化p53）的样品。 p53氧化还原产物的展开状态已进行了进一步的研究，以进行基于标记的银溶出伏安法。分光光度分析的结果显示，每种构象在不同波长处的吸收峰不同，这表明使用此技术来区分所测试的不同p53氧化还原产物的可能性。此外，这些结果似乎得到了基于结合亲和标记的测试的良好支持。总体而言，该研究表明可以通过这种简单且非侵入性的方法确定p53不同构象状态的可能性，从而降低了常规方法所涉及程序的复杂性。

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