Evidence map›Paper›PMID 30957356›Full record

ArticleAngewandte Chemie (International ed. in English)2019

Orthogonal Halogen-Bonding-Driven 3D Supramolecular Assembly of Right-Handed Synthetic Helical Peptides.

Peng Teng, Geoffrey M Gray, Mengmeng Zheng, Sylvia Singh, Xiaopeng Li, Lukasz Wojtas, Arjan van der Vaart, Jianfeng Cai

Open access · greenAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.7field-weighted citation impact, top 10% of its field
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

17 citing papers in PubMed, 51 citations in OpenAlex.

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  8. Peptidomimetic-based antibody surrogate for HER2.Acta pharmaceutica Sinica. B · 2021
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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

8 authors at 1 institution in 1 country.

Peng TengDepartment of Chemistry, University of South Florida, 4202 East Fowler Avenue, Tampa, FL, 33620, USA.ORCID 0000-0002-7412-9646
Geoffrey M GrayDepartment of Chemistry, University of South Florida, 4202 East Fowler Avenue, Tampa, FL, 33620, USA.
Mengmeng ZhengDepartment of Chemistry, University of South Florida, 4202 East Fowler Avenue, Tampa, FL, 33620, USA.
Sylvia SinghDepartment of Chemistry, University of South Florida, 4202 East Fowler Avenue, Tampa, FL, 33620, USA.
Xiaopeng LiDepartment of Chemistry, University of South Florida, 4202 East Fowler Avenue, Tampa, FL, 33620, USA.ORCID 0000-0001-9655-9551
Lukasz WojtasDepartment of Chemistry, University of South Florida, 4202 East Fowler Avenue, Tampa, FL, 33620, USA.
Arjan van der VaartDepartment of Chemistry, University of South Florida, 4202 East Fowler Avenue, Tampa, FL, 33620, USA.ORCID 0000-0002-8950-1850
Jianfeng CaiDepartment of Chemistry, University of South Florida, 4202 East Fowler Avenue, Tampa, FL, 33620, USA.ORCID 0000-0003-3106-3306
University of South Florida · US

Funding

Requesting HPLC for the project of "Alpha-AApeptides as a Novel Class of Antimicrobial Biomaterials"R01GM112652 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI CAI, JIANFENG · 2015 to 2019
$1.5M
National Science Foundation CAREER 1351265National Science Foundation CHE-1346572National Science Foundation DMR-1531283National Science Foundation MRI CHE-1531590NIGMS NIH HHS R01 GM112652NIH HHS 1R01GM112652-01A1
6 · The paper itself

Abstract

Peptide-mediated self-assembly is a prevalent method for creating highly ordered supramolecular architectures. Herein, we report the first example of orthogonal C-X⋅⋅⋅X-C/C-X⋅⋅⋅π halogen bonding and hydrogen bonding driven crystalline architectures based on synthetic helical peptides bearing hybrids of l-sulfono-γ-AApeptides and natural amino acids. The combination of halogen bonding, intra-/intermolecular hydrogen bonding, and intermolecular hydrophobic interactions enabled novel 3D supramolecular assembly. The orthogonal halogen bonding in the supramolecular architecture exerts a novel mechanism for the self-assembly of synthetic peptide foldamers and gives new insights into molecular recognition, supramolecular design, and rational design of biomimetic structures.

Indexed as

Protein FoldingBiomimetic MaterialsCrystallography, X-RayHalogensHumansHydrogen BondingHydrophobic and Hydrophilic InteractionsModels, MolecularPeptide FragmentsProtein ConformationHalogensPeptide Fragmentsfoldamershalogen bondingpeptidesself-assemblystructure elucidation

Identifiers

PMID30957356
PMCPMC6534470
OpenAlexW2938612142

What OpenQuestion holds

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Registered trials

None linked

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.