Evidence map›Paper›PMID 38391531›Full record

ArticleAntibiotics (Basel, Switzerland)2024

Study of the Antimicrobial Activity of the Human Peptide SQQ30 against Pathogenic Bacteria.

Michela Di Napoli, Giusy Castagliuolo, Sara Pio, Ilaria Di Nardo, Teresa Russo, Dario Antonini, Eugenio Notomista, Mario Varcamonti, Anna Zanfardino

Open access · goldAbstract read
In one paragraph

Article in Antibiotics (Basel, Switzerland), 2024. 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
3.8field-weighted citation impact, top 7% 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, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Myristicin fromAntibiotics (Basel, Switzerland) · 2026
    Article
  4. Article
  5. Article
  6. South Tyrol (Italy)Molecules (Basel, Switzerland) · 2025
    Article
  7. Review
  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

9 authors at 2 institutions in 1 country.

Michela Di NapoliDepartment of Biology, University of Naples Federico II, 80126 Naples, Italy.
Giusy CastagliuoloDepartment of Biology, University of Naples Federico II, 80126 Naples, Italy.
Sara PioDepartment of Biology, University of Naples Federico II, 80126 Naples, Italy.
Ilaria Di NardoDepartment of Biology, University of Naples Federico II, 80126 Naples, Italy.
Teresa RussoIPCB-Institute for Polymers, Composites and Biomaterials, National Research Council of Italy, 80125 Naples, Italy.
Dario AntoniniDepartment of Biology, University of Naples Federico II, 80126 Naples, Italy.
Eugenio NotomistaDepartment of Biology, University of Naples Federico II, 80126 Naples, Italy.ORCID 0000-0003-0097-6487
Mario VarcamontiDepartment of Biology, University of Naples Federico II, 80126 Naples, Italy.
Anna ZanfardinoDepartment of Biology, University of Naples Federico II, 80126 Naples, Italy.ORCID 0000-0002-6689-8365
University of Naples Federico II · ITNational Research Council · IT

Funding

MIUR Ministero dell'Università e della Ricerca, PRIN 2020 E65F22000370001
6 · The paper itself

Abstract

Given the continuous increase in antibiotic resistance, research has been driven towards the isolation of new antimicrobial molecules. Short, charged, and very hydrophobic antimicrobial peptides have a direct action against biological membranes, which are less prone to developing resistance. Using a bioinformatic tool, we chose the SQQ30 peptide, isolated from the human SOGA1 protein. The antimicrobial activity of this peptide against various Gram-negative and Gram-positive bacterial strains and against a fungal strain was studied. A mechanism of action directed against biological membranes was outlined. When administered in combination with the antibiotic ciprofloxacin and with the TRS21 (buforin II), another antimicrobial peptide, SQQ30 can be used with a lower MIC, showing additivity and synergism, respectively. Particularly interesting is the ability of SQQ30 to bind LPS in Gram-negative strains, preventing the eukaryotic cell from releasing inflammatory mediators. Our study indicates SQQ30 as a novel and promising antimicrobial agent.

Indexed as

antimicrobial activitybiological propertieshuman peptide

Identifiers

PMID38391531
PMCPMC10886087
OpenAlexW4391431765

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.