Evidence map›Paper›PMID 28756544›Full record

ArticleAmino acids2017

Retro analog concept: comparative study on physico-chemical and biological properties of selected antimicrobial peptides.

Damian Neubauer, Maciej Jaśkiewicz, Dorian Migoń, Marta Bauer, Karol Sikora, Emilia Sikorska, Elżbieta Kamysz, Wojciech Kamysz

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Amino acids, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

25 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
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  13. Effect of Camel Peptide on the Biofilm ofAntibiotics (Basel, Switzerland) · 2023
    Article
  14. Review
  15. Article
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  17. Article
  18. Review
  19. Article
  20. Recent Applications of Retro-Inverso Peptides.International journal of molecular sciences · 2021
    Review
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.

Damian NeubauerFaculty of Pharmacy, Medical University of Gdańsk, Gdańsk, Poland. dneu@gumed.edu.pl.ORCID 0000-0002-3230-6878
Maciej JaśkiewiczFaculty of Pharmacy, Medical University of Gdańsk, Gdańsk, Poland.
Dorian MigońFaculty of Pharmacy, Medical University of Gdańsk, Gdańsk, Poland.
Marta BauerFaculty of Pharmacy, Medical University of Gdańsk, Gdańsk, Poland.
Karol SikoraFaculty of Pharmacy, Medical University of Gdańsk, Gdańsk, Poland.
Emilia SikorskaFaculty of Chemistry, University of Gdańsk, Gdańsk, Poland.
Elżbieta KamyszFaculty of Chemistry, University of Gdańsk, Gdańsk, Poland.
Wojciech KamyszFaculty of Pharmacy, Medical University of Gdańsk, Gdańsk, Poland.
Gdańsk Medical University · PLUniversity of Gdańsk · PL

Funding

Narodowe Centrum Nauki 2011/03/B/NZ7/00548
6 · The paper itself

Abstract

Increasing drug resistance of common pathogens urgently needs discovery of new effective molecules. Antimicrobial peptides are believed to be one of the possible solutions of this problem. One of the approaches for improvement of biological properties is reversion of the sequence (retro analog concept). This research is based on investigation of antimicrobial activity against Gram-positive, Gram-negative bacteria, and fungi, hemolysis of erythrocytes, interpretation of the circular dichroism spectra, measurement of counter-ion content, and assessment of the peptide hydrophobicity and self-assembly using reversed-phase chromatography. The experiments were conducted using the following peptides: aurein 1.2, CAMEL, citropin 1.1, omiganan, pexiganan, temporin A, and their retro analogs. Among the compounds studied, only retro omiganan showed an enhanced antimicrobial and a slightly increased hemolytic activity as compared to parent molecule. Moreover, retro pexiganan exhibited high activity towards Klebsiella pneumoniae, whereas pexiganan was in general more or equally active against the rest of tested microorganisms. Furthermore, the determined activity was closely related to the peptide hydrophobicity. In general, the reduced hemolytic activity correlates with lower antimicrobial activity. The tendency to self-association and helicity fraction in SDS seems to be correlated. The normalized RP-HPLC-temperature profiles of citropin 1.1 and aurein 1.2, revealed an enhanced tendency to self-association than that of their retro analogs.

Indexed as

Amphibian ProteinsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesKlebsiella pneumoniaeAmphibian ProteinsAnti-Bacterial AgentsAntimicrobial Cationic Peptidesaurein 1.2 peptidecitropin 1.1 protein, LitoriaAntimicrobial peptidesCD experimentsOmigananPeptide hydrophobicityPexigananRetro analog

Identifiers

PMID28756544
PMCPMC5602100
OpenAlexW2739955608

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.