Evidence map›Paper›PMID 29040295›Full record

ArticlePloS one2017

Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4.

Ting-Wei Chang, Shu-Yi Wei, Shih-Han Wang, Hung-Mu Wei, Yu-June Wang, Chiu-Feng Wang, Chinpan Chen, You-Di Liao

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

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  8. Oreoch-1: A Peptide fromPathogens (Basel, Switzerland) · 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

8 authors at 1 institution in 1 country.

Ting-Wei ChangInstitute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan.
Shu-Yi WeiInstitute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan.
Shih-Han WangInstitute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan.
Hung-Mu WeiInstitute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan.
Yu-June WangInstitute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan.
Chiu-Feng WangInstitute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan.
Chinpan ChenInstitute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan.
You-Di LiaoInstitute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan.ORCID http://orcid.org/0000-0001-5527-4736
Institute of Biomedical Sciences, Academia Sinica · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antimicrobial peptides are important components of the host innate defense mechanism against invading pathogens, especially for drug-resistant bacteria. In addition to bactericidal activity, the 25 residue peptide TP4 isolated from Nile tilapia also stimulates cell proliferation and regulates the innate immune system in mice. In this report, TP4 hyperpolarized and depolarized the membrane potential of Pseudomonas aeruginosa at sub-lethal and lethal concentrations. It also inhibited and eradicated biofilm formation. The in vitro binding of TP4 to bacterial outer membrane target protein, OprI, was markedly enhanced by a membrane-like surfactant sarkosyl and lipopolysaccharide, which converted TP4 into an α-helix. The solution structure of TP4 in dodecylphosphocholine was solved by NMR analyses. It contained a typical α-helix at residues Phe10-Arg22 and a distorted helical segment at Ile6-Phe10, as well as a hydrophobic core at the N-terminus and a cationic patch at the C-terminus. Residues Ile16, Leu19 and Ile20 in the hydrophobic face of the main helix were critical for the integrity of amphipathic structure, other hydrophobic residues played important roles in hemolytic and bactericidal activities. A model for the assembly of helical TP4 embedded in sarkosyl vesicle is proposed. This study may provide valuable insight for engineering AMPs to have potent bactericidal activity but low hemolytic activity.

Indexed as

Amino Acid SequenceAnimalsAntimicrobial Cationic PeptidesBacterial ProteinsBiofilmsCandida albicansCell Membrane PermeabilityCichlidsErythrocytesFish ProteinsHydrophobic and Hydrophilic InteractionsLipopolysaccharidesLipoproteinsListeria monocytogenesMethicillin-Resistant Staphylococcus aureusMiceAntimicrobial Cationic PeptidesBacterial ProteinsdodecylphosphocholineFish ProteinsLipopolysaccharidesLipoproteinsouter membrane lipoprotein I, BacteriaPhosphorylcholineSarcosinesarkosyl

Identifiers

PMID29040295
PMCPMC5645128
OpenAlexW2765927862

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.