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氨基酸和肽的界面自组装:扫描隧道显微镜研究。

Interfacial self-assembly of amino acids and peptides: scanning tunneling microscopy investigation.

机构信息

Research Center for Bioengineering and Sensing Technology, University of Science & Technology Beijing, Beijing, 100083, PR China.

出版信息

Nanoscale. 2011 Dec;3(12):4901-15. doi: 10.1039/c1nr11070e. Epub 2011 Nov 4.

DOI:10.1039/c1nr11070e
PMID:22057641
Abstract

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.

摘要

蛋白质在人类日常生活中扮演着重要的角色。为了利用从自然界中获得的经验教训,研究蛋白质亚基(即氨基酸和多肽)的自组装至关重要。由于具有高分辨率和工作环境的多功能性,扫描隧道显微镜(STM)已成为研究界面分子组装结构的有力工具。本文旨在反映通过 STM 研究氨基酸和肽的界面自组装的进展。特别是,我们专注于环境诱导的多态性、手性识别以及与分子模板的共吸附行为。这些研究对于探索氨基酸和多肽在表面上的组装机制和纳米级控制分子组装、理解生命的起源、揭示分子水平疾病的本质以及确定构建具有有用性能和所需性能的分子器件和生物传感器的“自下而上”纳米制造所需的条件具有重要意义。

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Interfacial self-assembly of amino acids and peptides: scanning tunneling microscopy investigation.氨基酸和肽的界面自组装:扫描隧道显微镜研究。
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Surface modification and pattern formation by nucleobases and their coordination complexes.核碱基及其配位络合物的表面改性与图案形成
RSC Adv. 2018 Jul 6;8(43):24541-24560. doi: 10.1039/c8ra03903h. eCollection 2018 Jul 2.