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...
Autores principales: | , , , , |
---|---|
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 |