Evidence map›Paper›PMID 26156126›Full record

ArticleScientific reports2015

Functional Roles of Aromatic Residues and Helices of Papiliocin in its Antimicrobial and Anti-inflammatory Activities.

Eunjung Lee, Jin-Kyoung Kim, Dasom Jeon, Ki-Woong Jeong, Areum Shin, Yangmee Kim

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In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

38 citing papers in PubMed, 52 citations in OpenAlex.

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  13. Antiseptic 9-Meric Peptide with Potency against Carbapenem-ResistantInternational journal of molecular sciences · 2021
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  16. ACS infectious diseases · 2021
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  17. Review
  18. Identification and recombinant expression of an antimicrobial peptide (cecropin B-like) from soybean pestThe journal of venomous animals and toxins including tropical diseases · 2021
    Article
  19. Article
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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

6 authors at 1 institution in 1 country.

Eunjung LeeDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 143-701, South Korea.
Jin-Kyoung KimDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 143-701, South Korea.
Dasom JeonDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 143-701, South Korea.
Ki-Woong JeongDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 143-701, South Korea.
Areum ShinDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 143-701, South Korea.
Yangmee KimDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 143-701, South Korea.
Konkuk University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A cecropin-like peptide, papiliocin, isolated from the swallowtail butterfly Papilio xuthus, possesses high selectivity against gram-negative bacteria. Since Trp(2) and Phe(5) are highly conserved residues in cecropin-like peptides, we investigated the role of Trp(2) and Phe(5) in antibacterial activity. Substitution of Trp(2) and Phe(5) in papiliocin with Ala (papiliocin-2A and papiliocin-5A) revealed that Trp(2) is a key residue in its antibacterial activities. In order to understand the structural requirements for papiliocin function and to design shorter, but more potent, peptide antibiotics, we designed papiliocin constructs, PapN (residues Arg(1)-Ala(22) from the N-terminal amphipathic helix). PapN exhibited significant broad-spectrum antibacterial activities without cytotoxicity. Bactericidal kinetics of peptides against E.coli showed that papiliocin completely and rapidly killed E.coli in less than 10 minutes at 2× MIC concentration, while papiliocin-2A and papiliocin-5A killed four times more slowly than papiliocin. The PapN series peptides permeabilized bacterial membranes less effectively than papiliocin, showing no antibacterial activities in an hour. The results imply that the Trp(2) and Phe(5) in the amphipathic N-terminal helix are important in the rapid permeabilization of the gram-negative bacterial membrane. The hydrophobic C-terminal residues permeabilize the hydrophobic bacterial cell membrane synergistically with these aromatic residues, providing selectivity against gram-negative bacteria.

Indexed as

Amino Acid SequenceAnimalsAnti-Infective AgentsAnti-Inflammatory AgentsAntimicrobial Cationic PeptidesBacteriaButterfliesCell LineCell Membrane PermeabilityDose-Response Relationship, DrugHemolysisHumansMacrophagesMembrane PotentialsMiceMicrobial Sensitivity TestsAnti-Infective AgentsAnti-Inflammatory AgentsAntimicrobial Cationic PeptidesNitric Oxide

Identifiers

PMID26156126
PMCPMC4496781
OpenAlexW2265821154

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.