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Single molecule studies of cyclic peptides using molecular matrix at liquid/solid interface by scanning tunneling microscopy

机译:通过扫描隧道显微镜在液/固界面处使用分子基质对环肽进行单分子研究

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摘要

We report in this work the single molecule studies of cyclic peptide, cyclosporine A (CsA), using a molecular network formed by star-shaped oligofluorene (StOF-COOH_3) at the liquid/solid interface by scanning tunneling microscopy (STM). Individual cyclosporine A can be identified and resolved in the molecular network, and the high-resolution STM images of CsA show polygon-like characteristics with a diameter of approximately 1.7 nm. Furthermore, the complex of CsA and Mg~(2+) has also been observed to adsorb inside of the molecular matrix. The STM results reveal two adsorption characteristics for the CsA-Mg~(2+) complex, which is suggestive of asymmetrical configurations of the complex. The difference in binding energy between the two observed adsorption configurations is estimated to be 1.88 kJ?mol~(-1). These results help set the stage for studying the fine structures and functions of various cyclic peptides at the liquid/solid interface.
机译:我们在这项工作中报告了环肽,环孢菌素A(CsA)的单分子研究,它使用了由星形低聚芴(StOF-COOH_3)在液/固界面处通过扫描隧道显微镜(STM)形成的分子网络。可以在分子网络中识别并解析单个环孢菌素A,CsA的高分辨率STM图像显示直径约为1.7 nm的多边形状特征。此外,还观察到CsA和Mg〜(2+)的复合物吸附在分子基质内部。 STM结果揭示了CsA-Mg〜(2+)配合物的两个吸附特征,这表明该配合物的不对称构型。两种观察到的吸附构型之间的结合能差估计为1.88 kJ?mol〜(-1)。这些结果有助于为研究液体/固体界面上各种环肽的精细结构和功能奠定基础。

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