Evidence map›Paper›PMID 37218617›Full record

ArticleAngewandte Chemie (International ed. in English)2023

Crystal Structure and NMR of an α,δ-Peptide Foldamer Helix Shows Side-Chains are Well Placed for Bifunctional Catalysis: Application as a Minimalist Aldolase Mimic.

Qi Lin, Hao Lan, Chunmiao Ma, Ryan T Stendall, Kenneth Shankland, Rebecca A Musgrave, Peter N Horton, Carsten Baldauf, Hans-Jörg Hofmann, Craig P Butts and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

5 citing papers in PubMed, 18 citations in OpenAlex.

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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

12 authors at 7 institutions in 3 countries.

Qi LinDepartment of Chemistry, King's College London, 7 Trinity Street, London, SE1 1DB, UK.
Hao LanSchool of Chemistry, University of Bristol, Cantocks Close, Bristol, BS8 1TS, UK.
Chunmiao MaSchool of Chemistry and Chemical Engineering, Huazhong University of Science and Technology, Wuhan, 430074, P. R. China.
Ryan T StendallDepartment of Chemistry, King's College London, 7 Trinity Street, London, SE1 1DB, UK.
Kenneth ShanklandSchool of Chemistry, Food and Pharmacy (SCFP), University of Reading, Whiteknights Berks, Reading, RG6 6AD, UK.
Rebecca A MusgraveDepartment of Chemistry, King's College London, 7 Trinity Street, London, SE1 1DB, UK.
Peter N HortonEPSRC National Crystallography Service, School of Chemistry, University of Southampton Highfield, Southampton, SO17 1BJ, UK.
Carsten BaldaufFritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, 14195, Berlin, Germany.
Hans-Jörg HofmannInstitut für Biochemie, Universität Leipzig, Brüderstrasse 34, 04103, Leipzig, Germany.
Craig P ButtsSchool of Chemistry, University of Bristol, Cantocks Close, Bristol, BS8 1TS, UK.
Manuel M MüllerDepartment of Chemistry, King's College London, 7 Trinity Street, London, SE1 1DB, UK.
Alexander J A CobbDepartment of Chemistry, King's College London, 7 Trinity Street, London, SE1 1DB, UK.ORCID 0000-0002-3397-9636
King's College London · GBUniversity of Bristol · GBEngineering and Physical Sciences Research Council · GBFritz Haber Institute of the Max Planck Society · DEHuazhong University of Science and Technology · CNLeipzig University · DEUniversity of Reading · GB

Funding

Wellcome TrustWellcome Trust 202250/Z/16/Z
6 · The paper itself

Abstract

We report the first NMR and X-ray diffraction (XRD) structures of an unusual 13/11-helix (alternating i, i+1 {NH-O=C} and i, i+3 {C=O-H-N} H-bonds) formed by a heteromeric 1 : 1 sequence of α- and δ-amino acids, and demonstrate the application of this framework towards catalysis. Whilst intramolecular hydrogen bonds (IMHBs) are the clear driver of helix formation in this system, we also observe an apolar interaction between the ethyl residue of one δ-amino acid and the cyclohexyl group of the next δ-residue in the sequence that seems to stabilize one type of helix over another. To the best of our knowledge this type of additional stabilization leading to a specific helical preference has not been observed before. Critically, the helix type realized places the α-residue functionalities in positions proximal enough to engage in bifunctional catalysis as demonstrated in the application of our system as a minimalist aldolase mimic.

Indexed as

Fructose-Bisphosphate AldolasePeptidesAldehyde-LyasesAmino AcidsHydrogen BondingModels, MolecularAldehyde-LyasesAmino AcidsFructose-Bisphosphate AldolasePeptidesaldolasecatalysishelical conformationpeptidespeptidic foldamers

Identifiers

PMID37218617
PMCPMC10952276
OpenAlexW4377565390

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.