Evidence map›Paper›PMID 36421263›Full record

ArticleAntibiotics (Basel, Switzerland)2022

Design of Antimicrobial Peptides with Cell-Selective Activity and Membrane-Acting Mechanism against Drug-Resistant Bacteria.

Seong-Cheol Park, Hyosuk Son, Young-Min Kim, Jong-Kook Lee, Soyoung Park, Hye Song Lim, Jung Ro Lee, Mi-Kyeong Jang

Open access · goldAbstract read
In one paragraph

Article in Antibiotics (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

8 citing papers in PubMed, 18 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

8 authors at 2 institutions in 1 country.

Seong-Cheol ParkDepartment of Chemical Engineering, Sunchon National University, Suncheon 57922, Republic of Korea.ORCID 0000-0001-9051-0183
Hyosuk SonDepartment of Chemical Engineering, Sunchon National University, Suncheon 57922, Republic of Korea.
Young-Min KimDepartment of Chemical Engineering, Sunchon National University, Suncheon 57922, Republic of Korea.
Jong-Kook LeeDepartment of Chemical Engineering, Sunchon National University, Suncheon 57922, Republic of Korea.
Soyoung ParkDepartment of Chemical Engineering, Sunchon National University, Suncheon 57922, Republic of Korea.
Hye Song LimLMO Team, National Institute of Ecology (NIE), Seocheon 33657, Republic of Korea.
Jung Ro LeeLMO Team, National Institute of Ecology (NIE), Seocheon 33657, Republic of Korea.ORCID 0000-0002-9596-3330
Mi-Kyeong JangDepartment of Chemical Engineering, Sunchon National University, Suncheon 57922, Republic of Korea.
Sunchon National University · KRNational Institute of Ecology · KR

Funding

Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology NRF-2016R1D1A3A03918533National Institute of Ecology (NIE), funded by the Ministry of Environment (MOE) of Korea NIE-A-2022-07
6 · The paper itself

Abstract

Antimicrobial peptides (AMPs) can combat drug-resistant bacteria with their unique membrane-disruptive mechanisms. This study aimed to investigate the antibacterial effects of several membrane-acting peptides with amphipathic structures and positional alterations of two tryptophan residues. The synthetic peptides exhibited potent antibacterial activities in a length-dependent manner against various pathogenic drug-resistant and susceptible bacteria. In particular, the location of tryptophan near the N-terminus of AMPs simultaneously increases their antibacterial activity and toxicity. Furthermore, the growth inhibition mechanisms of these newly designed peptides involve cell penetration and destabilization of the cell membrane. These findings provide new insights into the design of peptides as antimicrobial agents and suggest that these peptides can be used as substitutes for conventional antibiotics.

Indexed as

antibacterial activitychimeric peptidecytotoxicitymembrane-acting mechanism

Identifiers

PMID36421263
PMCPMC9686514
OpenAlexW4309005032

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.