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Toward Methodology for Detection of Cancer-Promoting S100A4 Protein Conformations in Subnanomolar Concentrations Using Raman and SERS

机译:迈向使用拉曼和SERS检测亚纳摩尔浓度的促癌S100A4蛋白构象的方法论

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The cancer-promoting S100A4 protein has been studied using Raman and surface-enhanced Raman spectroscopy, RS and SERS, respectively. Two different forms of this protein, dimeric (MW≈ 26 kDa) and oligomeric (MW > 50 kDa), were purified and then individually studied in high concentration (ca. millimolar) by RS and in low concentration (ca. nanomolar) by SERS, to distinguish the characteristic vibrational modes of each species. The results have shown that a clear difference between these species was detectable, both by RS and by SERS. The nanomolar concentration used in this study is well representative of the average concentration of this protein in the plasma of healthy individuals. For SERS measurement, Ag-colloids were mixed with the protein solution, and a laser line of 532 nm was employed for all vibrational measurements. This is the first time that this cancer progression-promoting protein is studied by Raman and SERS spectroscopy and in as low concentrations as below nanomolar. Here, the novel results of the spectral analysis are presented and discussed.
机译:分别使用拉曼光谱和表面增强拉曼光谱,RS和SERS对促进癌症的S100A4蛋白进行了研究。纯化了两种不同形式的这种蛋白质,即二聚体(MW≈26 kDa)和寡聚体(MW> 50 kDa),然后分别通过RS在高浓度(ca. millimolar)和低浓度(ca. nanomolar)下进行单独研究。 ,以区分每种物质的特征振动模式。结果表明,通过RS和SERS均可检测到这些物种之间的明显差异。这项研究中使用的纳摩尔浓度很好地代表了健康个体血浆中该蛋白质的平均浓度。对于SERS测量,将Ag-胶体与蛋白质溶液混合,并使用532 nm的激光线进行所有振动测量。这是首次通过拉曼光谱和SERS光谱法研究这种促进癌症进展的蛋白质,其浓度低至纳摩尔以下。在这里,提出并讨论了光谱分析的新颖结果。

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