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Issue 12, 2011
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Interfacial self-assembly of amino acids and peptides: Scanning tunneling microscopy investigation

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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.

Graphical abstract: Interfacial self-assembly of amino acids and peptides: Scanning tunneling microscopy investigation

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Article information


Submitted
11 Aug 2011
Accepted
29 Sep 2011
First published
04 Nov 2011

Nanoscale, 2011,3, 4901-4915
Article type
Review Article

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

L. Xu, Y. Liu and X. Zhang, Nanoscale, 2011, 3, 4901
DOI: 10.1039/C1NR11070E

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