Evidence map›Paper›PMID 19805350›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Membrane structure and conformational changes of the antibiotic heterodimeric peptide distinctin by solid-state NMR spectroscopy.

Jarbas M Resende, Cléria Mendonça Moraes, Victor H O Munhoz, Christopher Aisenbrey, Rodrigo M Verly, Philippe Bertani, Amary Cesar, Dorila Piló-Veloso, Burkhard Bechinger

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Membrane Topology and Oligomerization of Peptaibols by Solid-State NMR Spectroscopy.Journal of peptide science : an official publication of the European Peptide Society · 2026
    Review
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  6. Review
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  13. Peptide-lipid interactions: experiments and applications.International journal of molecular sciences · 2013
    Article
  14. Article
  15. Antimicrobial properties of distinctin in an experimental model of MRSA-infected wounds.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2012
    Article
  16. Review
  17. Article
  18. Article
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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

9 authors.

Jarbas M ResendeUniversité de Strasbourg, Centre National de la Recherche Scientifique, UMR 7177, Institut de Chimie, 4 rue Blaise Pascal, Strasbourg, France.
Cléria Mendonça Moraes
Victor H O Munhoz
Christopher Aisenbrey
Rodrigo M Verly
Philippe Bertani
Amary Cesar
Dorila Piló-Veloso
Burkhard Bechinger

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The heterodimeric antimicrobial peptide distinctin is composed of 2 linear peptide chains of 22- and 25-aa residues that are connected by a single intermolecular S-S bond. This heterodimer has been considered to be a unique example of a previously unrecorded class of bioactive peptides. Here the 2 distinctin chains were prepared by chemical peptide synthesis in quantitative amounts and labeled with (15)N, as well as (15)N and (2)H, at selected residues, respectively, and the heterodimer was formed by oxidation. CD spectroscopy indicates a high content of helical secondary structures when associated with POPC/POPG 3:1 vesicles or in membrane-mimetic environments. The propensity for helix formation follows the order heterodimer >chain 2 >chain 1, suggesting that peptide-peptide and peptide-lipid interactions both help in stabilizing this secondary structure. In a subsequent step the peptides were reconstituted into oriented phospholipid bilayers and investigated by (2)H and proton-decoupled (15)N solid-state NMR spectroscopy. Whereas chain 2 stably inserts into the membrane at orientations close to perfectly parallel to the membrane surface in the presence or absence of chain 1, the latter adopts a more tilted alignment, which further increases in the heterodimer. The data suggest that membrane interactions result in considerable conformational rearrangements of the heterodimer. Therefore, chain 2 stably anchors the heterodimer in the membrane, whereas chain 1 interacts more loosely with the bilayer. These structural observations are consistent with the antimicrobial activities when the individual chains are compared to the dimer.

Indexed as

Amphibian ProteinsAnti-Infective AgentsAntimicrobial Cationic PeptidesCircular DichroismMembrane ProteinsModels, BiologicalNuclear Magnetic Resonance, BiomolecularOxidation-ReductionProtein ConformationAmphibian ProteinsAnti-Infective AgentsAntimicrobial Cationic PeptidesdistinctinMembrane Proteins

Identifiers

PMID19805350
PMCPMC2757838

What OpenQuestion holds

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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.