Evidence map›Paper›PMID 29379033›Full record

ArticleScientific reports2018

Mechanisms driving the antibacterial and antibiofilm properties of Hp1404 and its analogue peptides against multidrug-resistant Pseudomonas aeruginosa.

Min Kyung Kim, Hee Kyoung Kang, Su Jin Ko, Min Ji Hong, Jeong Kyu Bang, Chang Ho Seo, Yoonkyung Park

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

30 citing papers in PubMed, 61 citations in OpenAlex.

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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

7 authors at 3 institutions in 1 country.

Min Kyung KimResearch Center for proteineous Materials (RCPM), Chosun University, Kwangju, Republic of Korea.
Hee Kyoung KangDepartment of Biotechnology and BK21-Plus Research Team for Bioactive Control Technology, Chosun University, Kwangju, Republic of Korea.
Su Jin KoResearch Center for proteineous Materials (RCPM), Chosun University, Kwangju, Republic of Korea.
Min Ji HongResearch Center for proteineous Materials (RCPM), Chosun University, Kwangju, Republic of Korea.
Jeong Kyu BangDivision of Magnetic Resonance, Korea Basic Science Institute, Ochang, Chung-Buk, 363-883, Republic of Korea.
Chang Ho SeoDepartment of Bioinformatics, Kongju National University, Kongju, 314-701, South Korea.
Yoonkyung ParkResearch Center for proteineous Materials (RCPM), Chosun University, Kwangju, Republic of Korea. y_k_park@chosun.ac.kr.ORCID http://orcid.org/0000-0002-8717-3080
Chosun University · KRKongju National University · KRKorea Basic Science Institute · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hp1404, identified from the venom of the scorpion Heterometrus petersii, displays antimicrobial activity with cytotoxicity. Several synthetic peptides were designed based on the parent peptide Hp1404 to reduce cytotoxicity and improve activity (deletion of glycine and phenylalanine, substitution with leucine and lysine). The analogue peptides generated comprised 12 amino acids and displayed amphipathic α-helical structures, with higher hydrophobic moments and net positive charge than those of the Hp1404. The analogues showed less hemolytic and toxic effects toward mammalian cells than the Hp1404, especially Hp1404-T1e, which exhibited particularly potent antibacterial and antibiofilm activities against multidrug-resistant Pseudomonas aeruginosa (MRPA) strains. The analogue peptide Hp1404-T1e was more stable against salt and trypsin than the Hp1404. Hp1404's mechanism of action involves binding to lipopolysaccharide (LPS), thereby killing bacteria through membrane disruption. Hp1404-T1e kills bacteria more rapidly than Hp1404 and not only seems to bind more strongly to LPS but may also be able to enter bacterial cells and interact with their DNA. Additionally, Hp1404-T1e can effectively kill bacteria in vivo. The results of this study indicate that Hp1404-T1e not only displays antimicrobial activity, but is also functional in physiological conditions, confirming its potential use as an effective therapeutic agent against MRPA.

Indexed as

AnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBiofilmsCell LineCell MembraneDrug Resistance, Multiple, BacterialHumansLipopolysaccharidesMiceMice, Inbred BALB CMicrobial Sensitivity TestsPseudomonas aeruginosaAnti-Bacterial AgentsAntimicrobial Cationic PeptidesLipopolysaccharides

Identifiers

PMID29379033
PMCPMC5789083
OpenAlexW2794851462

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.