Evidence map›Paper›PMID 36878924›Full record

ArticleScientific reports2023

The impact of N-glycosylation on the properties of the antimicrobial peptide LL-III.

Attila Tortorella, Linda Leone, Angelina Lombardi, Elio Pizzo, Andrea Bosso, Roland Winter, Luigi Petraccone, Pompea Del Vecchio, Rosario Oliva

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Deep-Learning Driven Identification of Novel Antimicrobial Peptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  5. Review
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  8. Cliotide U1, a Novel Antimicrobial Peptide Isolated FromBioinformatics and biology insights · 2025
    Article
  9. Review
  10. Review
  11. Article
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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

9 authors at 4 institutions in 2 countries.

Attila TortorellaDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 26, 80126, Naples, Italy.
Linda LeoneDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 26, 80126, Naples, Italy.
Angelina LombardiDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 26, 80126, Naples, Italy.
Elio PizzoDepartment of Biology, University of Naples Federico II, Via Cintia 26, 80126, Naples, Italy.
Andrea BossoDepartment of Biology, University of Naples Federico II, Via Cintia 26, 80126, Naples, Italy.
Roland WinterFaculty of Chemistry and Chemical Biology, Biophysical Chemistry, TU Dortmund University, Otto-Hahn-Str. 4a, 44227, Dortmund, Germany.
Luigi PetracconeDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 26, 80126, Naples, Italy.
Pompea Del VecchioDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 26, 80126, Naples, Italy. pompea.delvecchio@unina.it.
Rosario OlivaDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 26, 80126, Naples, Italy. rosario.oliva2@unina.it.
University of Naples Federico II · ITScuola Superiore Meridionale · ITTecnologie Avanzate (Italy) · ITTU Dortmund University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The misuse of antibiotics has led to the emergence of drug-resistant pathogens. Antimicrobial peptides (AMPs) may represent valuable alternative to antibiotics; nevertheless, the easy degradation due to environmental stress and proteolytic enzyme action, limits their use. So far, different strategies have been developed to overcome this drawback. Among them, glycosylation of AMPs represents a promising approach. In this work, we synthesized and characterized the N-glycosilated form of the antimicrobial peptide LL-III (g-LL-III). The N-acetylglucosamine (NAG) was covalently linked to the Asn residue and the interaction of g-LL-III with bacterial model membranes, together with its resistance to proteases, were investigated. Glycosylation did not affect the peptide mechanism of action and its biological activity against both bacteria and eukaryotic cells. Interestingly, a higher resistance to the activity of proteolytic enzymes was achieved. The reported results pave the way for the successful application of AMPs in medicine and biotechnological fields.

Indexed as

Antimicrobial PeptidesEndopeptidasesAnti-Bacterial AgentsGlycosylationPeptide HydrolasesAnti-Bacterial AgentsAntimicrobial PeptidesEndopeptidasesPeptide Hydrolases

Identifiers

PMID36878924
PMCPMC9988962
OpenAlexW4323319329

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.