Cargando…

Tyrosine‐Rich Peptides as a Platform for Assembly and Material Synthesis

The self‐assembly of biomolecules can provide a new approach for the design of functional systems with a diverse range of hierarchical nanoarchitectures and atomically defined structures. In this regard, peptides, particularly short peptides, are attractive building blocks because of their ease of e...

Descripción completa

Detalles Bibliográficos
Autores principales: Lee, Jaehun, Ju, Misong, Cho, Ouk Hyun, Kim, Younghye, Nam, Ki Tae
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6382316/
https://www.ncbi.nlm.nih.gov/pubmed/30828522
http://dx.doi.org/10.1002/advs.201801255
_version_ 1783396650158391296
author Lee, Jaehun
Ju, Misong
Cho, Ouk Hyun
Kim, Younghye
Nam, Ki Tae
author_facet Lee, Jaehun
Ju, Misong
Cho, Ouk Hyun
Kim, Younghye
Nam, Ki Tae
author_sort Lee, Jaehun
collection PubMed
description The self‐assembly of biomolecules can provide a new approach for the design of functional systems with a diverse range of hierarchical nanoarchitectures and atomically defined structures. In this regard, peptides, particularly short peptides, are attractive building blocks because of their ease of establishing structure–property relationships, their productive synthesis, and the possibility of their hybridization with other motifs. Several assembling peptides, such as ionic‐complementary peptides, cyclic peptides, peptide amphiphiles, the Fmoc‐peptide, and aromatic dipeptides, are widely studied. Recently, studies on material synthesis and the application of tyrosine‐rich short peptide‐based systems have demonstrated that tyrosine units serve as not only excellent assembly motifs but also multifunctional templates. Tyrosine has a phenolic functional group that contributes to π–π interactions for conformation control and efficient charge transport by proton‐coupled electron‐transfer reactions in natural systems. Here, the critical roles of the tyrosine motif with respect to its electrochemical, chemical, and structural properties are discussed and recent discoveries and advances made in tyrosine‐rich short peptide systems from self‐assembled structures to peptide/inorganic hybrid materials are highlighted. A brief account of the opportunities in design optimization and the applications of tyrosine peptide‐based biomimetic materials is included.
format Online
Article
Text
id pubmed-6382316
institution National Center for Biotechnology Information
language English
publishDate 2018
publisher John Wiley and Sons Inc.
record_format MEDLINE/PubMed
spelling pubmed-63823162019-03-01 Tyrosine‐Rich Peptides as a Platform for Assembly and Material Synthesis Lee, Jaehun Ju, Misong Cho, Ouk Hyun Kim, Younghye Nam, Ki Tae Adv Sci (Weinh) Reviews The self‐assembly of biomolecules can provide a new approach for the design of functional systems with a diverse range of hierarchical nanoarchitectures and atomically defined structures. In this regard, peptides, particularly short peptides, are attractive building blocks because of their ease of establishing structure–property relationships, their productive synthesis, and the possibility of their hybridization with other motifs. Several assembling peptides, such as ionic‐complementary peptides, cyclic peptides, peptide amphiphiles, the Fmoc‐peptide, and aromatic dipeptides, are widely studied. Recently, studies on material synthesis and the application of tyrosine‐rich short peptide‐based systems have demonstrated that tyrosine units serve as not only excellent assembly motifs but also multifunctional templates. Tyrosine has a phenolic functional group that contributes to π–π interactions for conformation control and efficient charge transport by proton‐coupled electron‐transfer reactions in natural systems. Here, the critical roles of the tyrosine motif with respect to its electrochemical, chemical, and structural properties are discussed and recent discoveries and advances made in tyrosine‐rich short peptide systems from self‐assembled structures to peptide/inorganic hybrid materials are highlighted. A brief account of the opportunities in design optimization and the applications of tyrosine peptide‐based biomimetic materials is included. John Wiley and Sons Inc. 2018-11-15 /pmc/articles/PMC6382316/ /pubmed/30828522 http://dx.doi.org/10.1002/advs.201801255 Text en © 2018 The Authors. Published by WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Reviews
Lee, Jaehun
Ju, Misong
Cho, Ouk Hyun
Kim, Younghye
Nam, Ki Tae
Tyrosine‐Rich Peptides as a Platform for Assembly and Material Synthesis
title Tyrosine‐Rich Peptides as a Platform for Assembly and Material Synthesis
title_full Tyrosine‐Rich Peptides as a Platform for Assembly and Material Synthesis
title_fullStr Tyrosine‐Rich Peptides as a Platform for Assembly and Material Synthesis
title_full_unstemmed Tyrosine‐Rich Peptides as a Platform for Assembly and Material Synthesis
title_short Tyrosine‐Rich Peptides as a Platform for Assembly and Material Synthesis
title_sort tyrosine‐rich peptides as a platform for assembly and material synthesis
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6382316/
https://www.ncbi.nlm.nih.gov/pubmed/30828522
http://dx.doi.org/10.1002/advs.201801255
work_keys_str_mv AT leejaehun tyrosinerichpeptidesasaplatformforassemblyandmaterialsynthesis
AT jumisong tyrosinerichpeptidesasaplatformforassemblyandmaterialsynthesis
AT chooukhyun tyrosinerichpeptidesasaplatformforassemblyandmaterialsynthesis
AT kimyounghye tyrosinerichpeptidesasaplatformforassemblyandmaterialsynthesis
AT namkitae tyrosinerichpeptidesasaplatformforassemblyandmaterialsynthesis