Interfacial self-assembly of amino acids and peptides: scanning tunneling microscopy investigation.
Interfacial self-assembly of amino acids and peptides: scanning tunneling microscopy investigation.
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DOI：
10.1039/c1nr11070e
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发表时间：
2011-12
期刊：
影响因子：
6.7
通讯作者：
Li‐Ping Xu;Yibiao Liu;Xueji Zhang
中科院分区：
文献类型：
--
作者：
Li‐Ping Xu;Yibiao Liu;Xueji Zhang
蛋白质在人类日常生活中扮演着重要的角色。为了利用从自然中学到的经验教训，有必要研究蛋白质亚单位，即氨基酸和多肽的自组装。扫描隧道显微镜(STM)由于其高分辨率和工作环境的通用性，已成为研究界面分子组装结构的有力工具。本文综述了利用扫描隧道显微镜研究氨基酸和多肽的界面自组装的研究进展。特别是，我们关注环境诱导的多态、手性识别以及与分子模板的共吸附行为。这些研究将非常有益于探索氨基酸和多肽在表面上的机制和纳米级控制分子组装的研究努力，了解生命的起源，在分子水平上揭开疾病的本质，并认为需要什么才是正在构建的具有有用特性和期望性能的分子器件和生物传感器的“自下而上”纳米制造所必需的。
Proteins play important roles in human daily life. To take advantage of the lessons learned from nature, it is essential to investigate the self-assembly of subunits of proteins, i.e., amino acids and polypeptides. Due to its high resolution and versatility of working environment, scanning tunneling microscopy (STM) has become a powerful tool for studying interfacial molecular assembly structures. This review is intended to reflect the progress in studying interfacial self-assembly of amino acids and peptides by STM. In particular, we focus on environment-induced polymorphism, chiral recognition, and coadsorption behavior with molecular templates. These studies would be highly beneficial to research endeavors exploring the mechanism and nanoscale-controlling molecular assemblies of amino acids and polypeptides on surfaces, understanding the origin of life, unravelling the essence of disease at the molecular level and deeming what is necessary for the "bottom-up" nanofabrication of molecular devices and biosensors being constructed with useful properties and desired performance.