Evidence map›Paper›PMID 36671220›Full record

ArticleAntibiotics (Basel, Switzerland)2022

Structure-Activity Relationship Studies of Substitutions of Cationic Amino Acid Residues on Antimicrobial Peptides.

Mayu Takada, Takahito Ito, Megumi Kurashima, Natsumi Matsunaga, Yosuke Demizu, Takashi Misawa

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 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Candida albicans and Antifungal Peptides.Infectious diseases and therapy · 2023
    Article
  7. Article
  8. Article
  9. Article
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.

Mayu TakadaNational Institute of Health Sciences, 3-25-26, Tonomachi, Kawasaki-ku, Kawasaki-shi, Kanagawa 210-9501, Japan.
Takahito ItoNational Institute of Health Sciences, 3-25-26, Tonomachi, Kawasaki-ku, Kawasaki-shi, Kanagawa 210-9501, Japan.
Megumi KurashimaNational Institute of Health Sciences, 3-25-26, Tonomachi, Kawasaki-ku, Kawasaki-shi, Kanagawa 210-9501, Japan.
Natsumi MatsunagaNational Institute of Health Sciences, 3-25-26, Tonomachi, Kawasaki-ku, Kawasaki-shi, Kanagawa 210-9501, Japan.
Yosuke DemizuNational Institute of Health Sciences, 3-25-26, Tonomachi, Kawasaki-ku, Kawasaki-shi, Kanagawa 210-9501, Japan.ORCID 0000-0001-7521-4861
Takashi MisawaNational Institute of Health Sciences, 3-25-26, Tonomachi, Kawasaki-ku, Kawasaki-shi, Kanagawa 210-9501, Japan.
National Institute of Health Sciences · JP

Funding

the Japan Agency for Medical Research 256 and Development 22fk0108622j0002the Japan Agency for Medical Research and Development 21fk0108622j0001the Japan Agency for Medical Research and Development 22ak0101185j0301the Japan Agency for Medical Research and Development 22fk0210110j0401the Japan Agency for Medical Research and Development 22fk0310506j0701The japan Agency for medical research and development 22mk0101197j0002the Japan Society for the Promotion of Science and the Ministry of 258 Education, Culture, Sports, Science and Technology 20K06958the Japan Society for the Promotion of Science and the Ministry of 258 Education, Culture, Sports, Science and Technology 21K05320the Japan Society for the Promotion of Science and the Ministry of 258 Education, Culture, Sports, Science and Technology JP18H05502
6 · The paper itself

Abstract

Antimicrobial peptides (AMPs) have received considerable attention as next-generation drugs for infectious diseases. Amphipathicity and the formation of a stabilized secondary structure are required to exert their antimicrobial activity by insertion into the microbial membrane, resulting in lysis of the bacteria. We previously reported the development of a novel antimicrobial peptide, 17KKV, based on the Magainin 2 sequence. The peptide was obtained by increasing the amphipathicity due to the replacement of amino acid residues. Moreover, we studied the structural development of 17KKV and revealed that the secondary structural control of 17KKV by the introduction of non-proteinogenic amino acids such as α,α-disubstituted amino acids or side-chain stapling enhanced its antimicrobial activity. Among them, peptide

Indexed as

antimicrobial peptides (AMPs)cationic amino acidchemical stabilitydigestive enzymessecondary structure

Identifiers

PMID36671220
PMCPMC9854868
OpenAlexW4312175833

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.