Peptide Tectonics: Encoded Structural Complementarity Dictates Programmable Self-Assembly

Advanced Science
Shaofeng LouLinqi Shi

Abstract

Programmable self-assembly of peptides into well-defined nanostructures represents one promising approach for bioinspired and biomimetic synthesis of artificial complex systems and functional materials. Despite the progress made over the past two decades in the development of strategies for precise manipulation of the self-assembly of peptides, there is a remarkable gap between current peptide assemblies and biological systems in terms of structural complexity and functions. Here, the concept of peptide tectonics for the creation of well-defined nanostructures predominately driven by the complementary association at the interacting interfaces of tectons is introduced. Peptide tectons are defined as peptide building blocks exhibiting structural complementarity at the interacting interfaces of commensurate domains and undergoing programmable self-assembly into defined supramolecular structures promoted by complementary interactions. Peptide tectons are categorized based on their conformational entropy and the underlying mechanism for the programmable self-assembly of peptide tectons is highlighted focusing on the approaches for incorporating the structural complementarity within tectons. Peptide tectonics not only provides an alt...Continue Reading

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Citations

Feb 14, 2020·Microscopy and Microanalysis : the Official Journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada·Yaping LiFeng Zhang
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Jun 12, 2019·Bioconjugate Chemistry·Kazunori Matsuura, Takahide Honjo

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Methods Mentioned

BETA
Scanning electron microscopy
Transmission electron microscopy
atomic force microscopy
AFM
optical microscopy
circular dichroism

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