Evidence map›Paper›PMID 22253439›Full record

ArticleThe Journal of biological chemistry2012

Roles of hydrophobicity and charge distribution of cationic antimicrobial peptides in peptide-membrane interactions.

Lois M Yin, Michelle A Edwards, Jessica Li, Christopher M Yip, Charles M Deber

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 177 papers.

0numbers the graph read from it
0cells of the map it votes in
177citing papers in PubMed
12.5field-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

177 citing papers in PubMed, 410 citations in OpenAlex.

  1. Article
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  9. Epithelial sensing of vitamin A shapes intestinal antimicrobial defense.bioRxiv : the preprint server for biology · 2026
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  10. Review
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  14. Sphingolipid-mediated vesiculation in multidrug-resistantApplied and environmental microbiology · 2025
    Article
  15. Article
  16. Article
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  18. Review
  19. Article
  20. Resurfacing promotes antibacterial activity of a lipid A-binding nanobody.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article

117 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

5 authors at 1 institution in 1 country.

Lois M YinDivision of Molecular Structure and Function, Research Institute, Hospital for Sick Children, Toronto M5G 1X8, Canada.
Michelle A Edwards
Jessica Li
Christopher M Yip
Charles M Deber
University of Toronto · CA

Funding

Canadian Institutes of Health Research FRN-79284
6 · The paper itself

Abstract

Cationic antimicrobial peptides (CAPs) occur as important innate immunity agents in many organisms, including humans, and offer a viable alternative to conventional antibiotics, as they physically disrupt the bacterial membranes, leading to membrane lysis and eventually cell death. In this work, we studied the biophysical and microbiological characteristics of designed CAPs varying in hydrophobicity levels and charge distributions by a variety of biophysical and biochemical approaches, including in-tandem atomic force microscopy, attenuated total reflection-FTIR, CD spectroscopy, and SDS-PAGE. Peptide structural properties were correlated with their membrane-disruptive abilities and antimicrobial activities. In bacterial lipid model membranes, a time-dependent increase in aggregated β-strand-type structure in CAPs with relatively high hydrophobicity (such as KKKKKKALFALWLAFLA-NH(2)) was essentially absent in CAPs with lower hydrophobicity (such as KKKKKKAAFAAWAAFAA-NH(2)). Redistribution of positive charges by placing three Lys residues at both termini while maintaining identical sequences minimized self-aggregation above the dimer level. Peptides containing four Leu residues were destructive to mammalian model membranes, whereas those with corresponding Ala residues were not. This finding was mirrored in hemolysis studies in human erythrocytes, where Ala-only peptides displayed virtually no hemolysis up to 320 μM, but the four-Leu peptides induced 40-80% hemolysis at the same concentration range. All peptides studied displayed strong antimicrobial activity against Pseudomonas aeruginosa (minimum inhibitory concentrations of 4-32 μM). The overall findings suggest optimum routes to balancing peptide hydrophobicity and charge distribution that allow efficient penetration and disruption of the bacterial membranes without damage to mammalian (host) membranes.

Indexed as

Membranes, ArtificialAntimicrobial Cationic PeptidesBacteriaErythrocyte MembraneHemolysisHumansHydrophobic and Hydrophilic InteractionsProtein Structure, SecondaryAntimicrobial Cationic PeptidesMembranes, Artificial

Identifiers

PMID22253439
PMCPMC3293554
OpenAlexW1985816651

What OpenQuestion holds

Textmetadata
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.