Evidence map›Paper›PMID 20698568›Full record

ReviewACS chemical biology2010

Describing the mechanism of antimicrobial peptide action with the interfacial activity model.

William C Wimley

Abstract readReview
In one paragraph

Review in ACS chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 405 papers.

0numbers the graph read from it
0cells of the map it votes in
405citing 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

405 citing papers in PubMed.

  1. Review
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  16. Review
  17. Synergistic Action of Antimicrobial Peptides and Antibiotics.International journal of molecular sciences · 2026
    Review
  18. Review
  19. Article
  20. Article

345 more citing papers are in PubMed but not listed here.

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

1 author.

William C WimleyDepartment of Biochemistry SL43, Tulane University Health Sciences Center, New Orleans, Louisiana 70112-2699, USA. wwimley@tulane.edu

Funding

Folding and Design of Beta Sheets in MembranesR01GM060000 · NIGMS · TULANE UNIVERSITY OF LOUISIANA · PI WIMLEY, WILLIAM C · 2001 to 2010
$2.6M
NIGMS NIH HHS GM060000NIGMS NIH HHS R01 GM060000
6 · The paper itself

Abstract

Antimicrobial peptides (AMPs) have been studied for three decades, and yet a molecular understanding of their mechanism of action is still lacking. Here we summarize current knowledge for both synthetic vesicle experiments and microbe experiments, with a focus on comparisons between the two. Microbial experiments are done at peptide to lipid ratios that are at least 4 orders of magnitude higher than vesicle-based experiments. To close the gap between the two concentration regimes, we propose an "interfacial activity model", which is based on an experimentally testable molecular image of AMP-membrane interactions. The interfacial activity model may be useful in driving engineering and design of novel AMPs.

Indexed as

Amino Acid SequenceAnimalsAnti-Infective AgentsAntimicrobial Cationic PeptidesBacteriaBacterial InfectionsCell MembraneHumansMembranes, ArtificialModels, BiologicalModels, MolecularMolecular Sequence DataAnti-Infective AgentsAntimicrobial Cationic PeptidesMembranes, Artificial

Identifiers

PMID20698568
PMCPMC2955829

What OpenQuestion holds

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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.