Evidence map›Paper›PMID 32957844›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2020

Novel temporin L antimicrobial peptides: promoting self-assembling by lipidic tags to tackle superbugs.

Rosa Bellavita, Annarita Falanga, Elisabetta Buommino, Francesco Merlino, Bruno Casciaro, Floriana Cappiello, Maria Luisa Mangoni, Ettore Novellino, Maria Rosaria Catania, Rossella Paolillo and 2 more

Abstract read
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. An Overview of Supramolecular Platforms Boosting Drug Delivery.Bioinorganic chemistry and applications · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

12 authors.

Rosa BellavitaDepartment of Pharmacy, University of Naples "Federico II", Naples, Italy.ORCID https://orcid.org/0000-0003-2163-5163
Annarita FalangaDepartment of Agricultural Sciences, University of Naples "Federico II", Portici, Italy.ORCID https://orcid.org/0000-0001-6538-8585
Elisabetta BuomminoDepartment of Pharmacy, University of Naples "Federico II", Naples, Italy.ORCID https://orcid.org/0000-0002-9955-3179
Francesco MerlinoDepartment of Pharmacy, University of Naples "Federico II", Naples, Italy.ORCID https://orcid.org/0000-0002-9607-229X
Bruno CasciaroCenter for Life Nano Science@Sapienza, Italian Institute of Technology, Rome, Italy.ORCID https://orcid.org/0000-0003-1295-1084
Floriana CappielloDepartment of Biochemical Sciences, Laboratory affiliated to Pasteur Institute Italia-Fondazione Cenci Bolognetti, Sapienza University of Rome, Rome, Italy.
Maria Luisa MangoniDepartment of Biochemical Sciences, Laboratory affiliated to Pasteur Institute Italia-Fondazione Cenci Bolognetti, Sapienza University of Rome, Rome, Italy.ORCID https://orcid.org/0000-0002-5991-5868
Ettore NovellinoDepartment of Pharmacy, University of Naples "Federico II", Naples, Italy.ORCID https://orcid.org/0000-0002-2181-2142
Maria Rosaria CataniaDepartment of Molecular Medicine and Medical Biotechnologies, University of Naples "Federico II", Naples, Italy.ORCID https://orcid.org/0000-0002-8765-137X
Rossella PaolilloDepartment of Molecular Medicine and Medical Biotechnologies, University of Naples "Federico II", Naples, Italy.
Paolo GriecoDepartment of Pharmacy, University of Naples "Federico II", Naples, Italy.ORCID https://orcid.org/0000-0002-6854-8123
Stefania GaldieroaDepartment of Pharmacy, University of Naples "Federico II", Naples, Italy.ORCID https://orcid.org/0000-0002-7849-7024

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The rapid development of antimicrobial resistance is pushing the search in the discovering of novel antimicrobial molecules to prevent and treat bacterial infections. Self-assembling antimicrobial peptides, as the lipidated peptides, are a novel and promising class of molecules capable of meeting this need. Based on previous work on Temporin L analogs, several new molecules lipidated at the N- or and the C-terminus were synthesised. Our goal is to improve membrane interactions through finely tuning self-assembly to reduce oligomerisation in aqueous solution and enhance self-assembly in bacterial membranes while reducing toxicity against human cells. The results here reported show that the length of the aliphatic moiety is a key factor to control target cell specificity and the oligomeric state of peptides either in aqueous solution or in a membrane-mimicking environment. The results of this study pave the way for the design of novel molecules with enhanced activities.

Indexed as

AnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesCells, CulturedCell SurvivalDose-Response Relationship, DrugHumansKlebsiella pneumoniaeMicrobial Sensitivity TestsMolecular StructureProteolysisPseudomonas aeruginosaSheepStaphylococcus aureusStructure-Activity RelationshipAnti-Bacterial AgentsAntimicrobial Cationic Peptidestemporin L, Rana temporariaAntimicrobial peptides (AMPs)membrane interactionself-assemblingtemporin L analogues

Identifiers

PMID32957844
PMCPMC7534258

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.