Evidence map›Paper›PMID 34208826›Full record

ArticleInternational journal of molecular sciences2021

Peptide/β-Peptoid Hybrids with Ultrashort PEG-Like Moieties: Effects on Hydrophobicity, Antibacterial Activity and Hemolytic Properties.

Nicki Frederiksen, Stavroula Louka, Chirag Mudaliar, Ilona Domraceva, Agrita Kreicberga, Osvalds Pugovics, Dorota Żabicka, Magdalena Tomczak, Weronika Wygoda, Fredrik Björkling and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Fmoc Solid-Phase Peptide Synthesis.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  4. 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

11 authors.

Nicki FrederiksenCenter for Peptide-Based Antibiotics, Department of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, DK-2100 Copenhagen, Denmark.ORCID 0000-0002-7089-5909
Stavroula LoukaCenter for Peptide-Based Antibiotics, Department of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, DK-2100 Copenhagen, Denmark.
Chirag MudaliarCenter for Peptide-Based Antibiotics, Department of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, DK-2100 Copenhagen, Denmark.
Ilona DomracevaLatvian Institute of Organic Synthesis, Aizkraukles 21, 1006 Riga, Latvia.
Agrita KreicbergaLatvian Institute of Organic Synthesis, Aizkraukles 21, 1006 Riga, Latvia.
Osvalds PugovicsLatvian Institute of Organic Synthesis, Aizkraukles 21, 1006 Riga, Latvia.
Dorota ŻabickaDepartment of Epidemiology and Clinical Microbiology, National Medicines Institute, ul. Chełmska 30/34, 00-725 Warsaw, Poland.ORCID 0000-0001-9386-8885
Magdalena TomczakDepartment of Epidemiology and Clinical Microbiology, National Medicines Institute, ul. Chełmska 30/34, 00-725 Warsaw, Poland.
Weronika WygodaDepartment of Epidemiology and Clinical Microbiology, National Medicines Institute, ul. Chełmska 30/34, 00-725 Warsaw, Poland.ORCID 0000-0002-3921-3287
Fredrik BjörklingCenter for Peptide-Based Antibiotics, Department of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, DK-2100 Copenhagen, Denmark.
Henrik FranzykCenter for Peptide-Based Antibiotics, Department of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, DK-2100 Copenhagen, Denmark.ORCID 0000-0002-2822-1927

Funding

Novo Nordisk Fonden NNF16OC0021700
6 · The paper itself

Abstract

PEGylation of antimicrobial peptides as a shielding tool that increases stability toward proteolytic degradation typically leads to concomitant loss of activity, whereas incorporation of ultrashort PEG-like amino acids (sPEGs) remains essentially unexplored. Here, modification of a peptide/β-peptoid hybrid with sPEGs was examined with respect to influence on hydrophobicity, antibacterial activity and effect on viability of mammalian cells for a set of 18 oligomers. Intriguingly, the degree of sPEG modification did not significantly affect hydrophobicity as measured by retention in reverse-phase HPLC. Antibacterial activity against both wild-type and drug-resistant strains of

Indexed as

Acinetobacter baumanniiAnti-Bacterial AgentsCell SurvivalDrug Resistance, BacterialEscherichia coliHemolysisHep G2 CellsHumansHydrophobic and Hydrophilic InteractionsMicrobial Sensitivity TestsMolecular StructurePeptidomimeticsPeptoidsPolyethylene GlycolsAnti-Bacterial AgentsPeptidomimeticsPeptoidsPolyethylene Glycolsantibacterial activityhemolysisHepG2 cell viabilityhydrophobicitypeptidomimeticsultrashort PEG-like moieties

Identifiers

PMID34208826
PMCPMC8268887

What OpenQuestion holds

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LicenceCC BY
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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.