Evidence map›Paper›PMID 42464481›Full record

ArticleAngewandte Chemie (International ed. in English)2026

Azole γ-Peptides Helix Switching via Heterocycle Substitutions.

Samantha Chaise, Claude Didierjean, Audrey Gacogne, Maxime Fillaudeau, Young Kee Kang, Aurélien Lebrun, Jean-Louis Bantignies, Dominique Housset, Muriel Amblard, Ludovic T Maillard and 1 more

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

11 authors.

Samantha ChaiseIBMM, UMR5247, Univ. Montpellier, CNRS, ENSCM, Montpellier, France.
Claude DidierjeanCRM2, Université de Lorraine, CNRS, Nancy, France.ORCID 0000-0002-3176-8974
Audrey GacogneIBMM, UMR5247, Univ. Montpellier, CNRS, ENSCM, Montpellier, France.
Maxime FillaudeauIBMM, UMR5247, Univ. Montpellier, CNRS, ENSCM, Montpellier, France.
Young Kee KangDepartment of Chemistry, Chungbuk National University, Cheongju, Chungbuk, Republic of Korea.ORCID 0000-0002-2200-8922
Aurélien LebrunPAC Chimie Balard, Univ. Montpellier, CNRS, ENSCM, Montpellier, France.
Jean-Louis BantigniesL2C, UMR5221, Univ. Montpellier, CNRS, Montpellier, France.
Dominique HoussetIBS, Université Grenoble Alpes, CEA, CNRS, Grenoble, France.
Muriel AmblardIBMM, UMR5247, Univ. Montpellier, CNRS, ENSCM, Montpellier, France.ORCID 0000-0001-8922-1755
Ludovic T MaillardIBMM, UMR5247, Univ. Montpellier, CNRS, ENSCM, Montpellier, France.ORCID 0000-0002-9437-9765
Baptiste LegrandIBMM, UMR5247, Univ. Montpellier, CNRS, ENSCM, Montpellier, France.ORCID 0000-0001-8931-7757

Funding

ANR ANR-21-CE07-0039CNRSPAC Chimie Balard IBMM UMR 5247 MontpellierPAC Chimie Balard UAR CNRS 2041
6 · The paper itself

Abstract

Precise control of peptide backbone folding through non-covalent interactions remains a major challenge in foldamer design. In this work, we demonstrate that heteroatom substitutions program conformational switching in azole γ-peptides by tuning intrinsic stereoelectronic effects within heterocyclic γ-amino acids. Conformationally constrained thiazole- and oxazole-based γ-amino acids were designed to adopt conformations driven by either a C

Indexed as

AzolesHeterocyclic CompoundsPeptidesHydrogen BondingAzolesHeterocyclic CompoundsPeptidesfoldamershelix switchingheterocyclesstereoelectronic controlγ‐peptides

Identifiers

PMID42464481
PMCPMC13528534

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.