Evidence map›Paper›PMID 30828522›Full record

ReviewAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2019

Tyrosine-Rich Peptides as a Platform for Assembly and Material Synthesis.

Jaehun Lee, Misong Ju, Ouk Hyun Cho, Younghye Kim, Ki Tae Nam

Abstract readReview
In one paragraph

Review in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

50 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Jaehun LeeDepartment of Materials Science and Engineering Seoul National University Seoul 08826 Republic of Korea.
Misong JuDepartment of Materials Science and Engineering Seoul National University Seoul 08826 Republic of Korea.
Ouk Hyun ChoDepartment of Materials Science and Engineering Seoul National University Seoul 08826 Republic of Korea.
Younghye KimDepartment of Materials Science and Engineering Seoul National University Seoul 08826 Republic of Korea.
Ki Tae NamDepartment of Materials Science and Engineering Seoul National University Seoul 08826 Republic of Korea.ORCID https://orcid.org/0000-0001-6353-8877

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

peptide assemblypeptide‐based hybrid materialstyrosinetyrosine‐rich peptides

Identifiers

PMID30828522
PMCPMC6382316

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.