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Spatial recognition and mapping of proteins using DNA aptamers

机译：使用DNA适体对蛋白质进行空间识别和定位

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Atomic force microscopy-based adhesion force measurements have emerged as a powerful tool for the biophysical analyses of biological systems. Such measurements can now be extended to detection and mapping of biomolecules on surfaces via integrated imaging and force spectroscopy techniques. Critical to these experiments is the choice of the biomolecular recognition probe. In this study, we demonstrate how oligonucleotide aptamers can be used as versatile probes to simultaneously image and spatially locate targets on surfaces. We focus on two structurally distinct proteins relevant to the clotting cascade-human α-thrombin and vascular endothelial growth factor. Via AFM-recognition mapping using specific DNA aptamers on a commercially available instrument, we show a clear consistency between height and force measurements obtained simultaneously. Importantly, we are able to observe changes in binding due to changes in the external microenvironment, which demonstrate the ability to study fluctuating biological systems in real time. The aptamer specificity and the ability to distinguish their targets are shown through positive and negative controls. It is therefore possible to generate high resolution maps to spatially and temporally identify proteins at the molecular level on complex surfaces.
机译：基于原子力显微镜的粘附力测量已成为一种对生物系统进行生物物理分析的强大工具。这样的测量现在可以扩展到通过集成成像和力谱技术检测和绘制表面上的生物分子。这些实验的关键是生物分子识别探针的选择。在这项研究中，我们演示了如何将寡核苷酸适体用作通用探针，以同时对表面上的目标进行成像和空间定位。我们专注于与凝血级联人α-凝血酶和血管内皮生长因子相关的两种结构上不同的蛋白质。通过使用市售仪器上的特定DNA适体进行AFM识别作图，我们显示了同时获得的高度和力测量之间的明显一致性。重要的是，我们能够观察到由于外部微环境的变化而引起的结合力变化，这表明了能够实时研究波动的生物系统的能力。通过阳性和阴性对照显示适体特异性和区分其靶标的能力。因此，可以生成高分辨率图，以在空间和时间上识别复杂表面上分子水平的蛋白质。

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