Evidence map›Paper›PMID 20387900›Full record

ArticleBiochemistry2010

Probing the "charge cluster mechanism" in amphipathic helical cationic antimicrobial peptides.

Raquel F Epand, W Lee Maloy, Ayyalusamy Ramamoorthy, Richard M Epand

Abstract read
In one paragraph

Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
9.9field-weighted citation impact, top 1% 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

60 citing papers in PubMed, 151 citations in OpenAlex.

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  14. EcDBS1R4, an Antimicrobial Peptide Effective againstInternational journal of molecular sciences · 2020
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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

4 authors at 3 institutions in 2 countries.

Raquel F EpandDepartment of Biochemistry and Biomedical Sciences, McMaster University Health Sciences Centre, Hamilton, Ontario L8N 3Z5, Canada.
W Lee Maloy
Ayyalusamy Ramamoorthy
Richard M Epand
Health Sciences Centre · CAGenaera (United States) · USUniversity of Michigan–Ann Arbor · US

Funding

Structure and function of antimicrobial peptidesR01AI054515 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2004 to 2008
$1.3M
CIHR MOP 86608NIAID NIH HHS AI054515NIAID NIH HHS R01 AI054515
6 · The paper itself

Abstract

Clustering of anionic lipids away from zwitterionic ones by cationic antimicrobial agents has recently been established as a mechanism of action of natural small, flexible peptides as well as non-natural synthetic peptide mimics. One of the largest classes of antimicrobial peptides consists of peptides that form cationic amphipathic helices on membranes and whose toxic action is dependent on the formation of pores in the membrane or through the "carpet" mechanism. We have evaluated the role of anionic lipid clustering for five of these peptides, i.e., MSI-78, MSI-103, MSI-469, MSI-843, and MSI-1254, with different sequences and properties. We determined whether these amphipathic helical cationic antimicrobial peptides cluster anionic lipids from zwitterionic ones and if this property is related to the species specificity of their toxicity. All five of these peptides were capable of lipid clustering, in contrast to the well-studied amphipathic helical antimicrobial peptide, magainin 2, which does not. We ascribe this difference to the lower density of positive charges in magainin 2. Peptides that efficiently cluster anionic lipids generally have a ratio of MIC for Staphylococcus aureus to that for Escherichia coli of >1. The addition of an N-terminal octyl chain did not preclude anionic charge clustering, although the ratio of MIC for S. aureus to that for E. coli was somewhat lowered. In most Gram-positive bacteria, there is a predominance of anionic lipids in the cytoplasmic membrane. In Gram-negative bacteria, however, clustering of anionic lipids away from zwitterionic ones is emerging as an important contributing mechanism of bacterial toxicity for some antimicrobial agents.

Indexed as

Antimicrobial Cationic PeptidesCell MembraneCell Membrane PermeabilityEscherichia coliPeptidesStaphylococcus aureusAntimicrobial Cationic PeptidesPeptides

Identifiers

PMID20387900
PMCPMC2868066
OpenAlexW2092469155

What OpenQuestion holds

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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.