Evidence map›Paper›PMID 33411956›Full record

ArticleChembiochem : a European journal of chemical biology2021

Insight into the Mechanism of Action and Peptide-Membrane Interactions of Aib-Rich Peptides: Multitechnique Experimental and Theoretical Analysis.

Maria Giovanna Lizio, Mario Campana, Matteo De Poli, Damien F Jefferies, William Cullen, Valery Andrushchenko, Nikola P Chmel, Petr Bouř, Syma Khalid, Jonathan Clayden and 3 more

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2021. 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
–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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. A ChiralJournal of the American Chemical Society · 2022
    Article
  5. Article
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

13 authors.

Maria Giovanna LizioDepartment of Chemistry, University of Warwick, Coventry, CV4 7AL, UK.
Mario CampanaISIS Neutron and Muon Source, Rutherford Appleton Laboratory Harwell Didcot, Oxford, OX11 0QX, UK.
Matteo De PoliDepartment of Chemistry, University of Manchester, Oxford Road, Manchester, M13 9PL, UK.
Damien F JefferiesSchool of Chemistry, University of Southampton Highfield, Southampton, SO17 1BJ, UK.
William CullenDepartment of Chemistry, University of Manchester, Oxford Road, Manchester, M13 9PL, UK.
Valery AndrushchenkoInstitute of Organic Chemistry and Biochemistry, Academy of Sciences, Flemingovo náměstí 2, 16610, Prague 6, Czech Republic.
Nikola P ChmelDepartment of Chemistry, University of Warwick, Coventry, CV4 7AL, UK.
Petr BouřInstitute of Organic Chemistry and Biochemistry, Academy of Sciences, Flemingovo náměstí 2, 16610, Prague 6, Czech Republic.
Syma KhalidSchool of Chemistry, University of Southampton Highfield, Southampton, SO17 1BJ, UK.
Jonathan ClaydenSchool of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK.
Ewan BlanchSchool of Science, RMIT University, GPO Box 2476, Melbourne, Victoria, 3001, Australia.
Alison RodgerDepartment of Chemistry, University of Warwick, Coventry, CV4 7AL, UK.
Simon J WebbDepartment of Chemistry, University of Manchester, Oxford Road, Manchester, M13 9PL, UK.

Funding

Czech Ministry of Education CZ.02.1.01/0.0/0.0/16_019/0000729EPSRC EP/N009134/1EPSRC EP/P027067/1European Research Council ROCOCOINTER 1910639STFC Rutherford Appleton Laboratory 1600026
6 · The paper itself

Abstract

The increase in resistant bacterial strains necessitates the identification of new antimicrobial molecules. Antimicrobial peptides (AMPs) are an attractive option because of evidence that bacteria cannot easily develop resistance to AMPs. The peptaibols, a class of naturally occurring AMPs, have shown particular promise as antimicrobial drugs, but their development has been hindered by their mechanism of action not being clearly understood. To explore how peptaibols might interact with membranes, circular dichroism, vibrational circular dichroism, linear dichroism, Raman spectroscopy, Raman optical activity, neutron reflectivity and molecular dynamics simulations have been used to study a small library of peptaibol mimics, the Aib-rich peptides. All the peptides studied quickly partitioned and oriented in membranes, and we found evidence of chiral interactions between the phospholipids and membrane-embedded peptides. The protocols presented in this paper open new ground by showing how chiro-optical spectroscopies can throw light on the mechanism of action of AMPs.

Indexed as

Molecular Dynamics SimulationAntimicrobial Cationic PeptidesCircular DichroismLipid BilayersPeptaibolsPhosphatidylcholinesStereoisomerism1,2-oleoylphosphatidylcholineAntimicrobial Cationic PeptidesLipid BilayersPeptaibolsPhosphatidylcholinesantimicrobial peptideslipid-peptide interactionsmembranesmolecular dynamicspeptaibolstransfer of chirality

Identifiers

PMID33411956
PMCPMC8248331

What OpenQuestion holds

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LicenceCC BY
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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.