Evidence map›Paper›PMID 32038530›Full record

ArticleFrontiers in microbiology2019

Mechanism of Action of Surface Immobilized Antimicrobial Peptides Against

Muhammad Yasir, Debarun Dutta, Khondker R Hossain, Renxun Chen, Kitty K K Ho, Rajesh Kuppusamy, Ronald J Clarke, Naresh Kumar, Mark D P Willcox

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
7.3field-weighted citation impact, top 2% 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

36 citing papers in PubMed, 79 citations in OpenAlex.

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  19. Anti-Microorganisms · 2023
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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 at 3 institutions in 2 countries.

Muhammad YasirSchool of Optometry and Vision Science, University of New South Wales, Sydney, NSW, Australia.
Debarun DuttaSchool of Optometry and Vision Science, University of New South Wales, Sydney, NSW, Australia.
Khondker R HossainSchool of Chemistry, The University of Sydney Nano Institute, The University of Sydney, Sydney, NSW, Australia.
Renxun ChenSchool of Chemistry, University of New South Wales, Sydney, NSW, Australia.
Kitty K K HoSchool of Chemistry, University of New South Wales, Sydney, NSW, Australia.
Rajesh KuppusamySchool of Chemistry, University of New South Wales, Sydney, NSW, Australia.
Ronald J ClarkeSchool of Chemistry, The University of Sydney Nano Institute, The University of Sydney, Sydney, NSW, Australia.
Naresh KumarSchool of Chemistry, University of New South Wales, Sydney, NSW, Australia.
Mark D P WillcoxSchool of Optometry and Vision Science, University of New South Wales, Sydney, NSW, Australia.
UNSW Sydney · AUUniversity of Sydney · AUAston University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial colonization and biofilm development on medical devices can lead to infection. Antimicrobial peptide-coated surfaces may prevent such infections. Melimine and Mel4 are chimeric cationic peptides showing broad-spectrum antimicrobial activity once attached to biomaterials and are highly biocompatible in animal models and have been tested in Phase I and II/III human clinical trials. These peptides were covalently attached to glass using an azidobenzoic acid linker. Peptide attachment was confirmed using X-ray photoelectron spectroscopy and amino acid analysis. Mel4 when bound to glass was able to adopt a more ordered structure in the presence of bacterial membrane mimetic lipids. The ability of surface bound peptides to neutralize endotoxin was measured along with their interactions with the bacterial cytoplasmic membrane which were analyzed using DiSC(3)-5 and Sytox green, Syto-9, and PI dyes with fluorescence microscopy. Leakage of ATP and nucleic acids from cells were determined by analyzing the surrounding fluid. Attachment of the peptides resulted in increases in the percentage of nitrogen by 3.0% and 2.4%, and amino acid concentrations to 0.237 nmole and 0.298 nmole per coverslip on melimine and Mel4 coated surfaces, respectively. The immobilized peptides bound lipopolysaccharide and disrupted the cytoplasmic membrane potential of

Indexed as

antimicrobial peptidesmembrane disruptionmode of actionPseudomonas aeruginosasurface immobilization

Identifiers

PMID32038530
PMCPMC6987417
OpenAlexW3001428210

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.