Evidence map›Paper›PMID 39409150›Full record

ReviewInternational journal of molecular sciences2024

Enhancing Antimicrobial Peptide Activity through Modifications of Charge, Hydrophobicity, and Structure.

Przemysław Gagat, Michał Ostrówka, Anna Duda-Madej, Paweł Mackiewicz

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing 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

79 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Biomolecules · 2026
    Article
  5. Article
  6. Activity of Secondary Metabolites from Marine-DerivedInternational journal of molecular sciences · 2026
    Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. Article

19 more citing papers are in PubMed but not listed here.

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

4 authors.

Przemysław GagatFaculty of Biotechnology, University of Wroclaw, Fryderyka Joliot-Curie 14a, 50-137 Wroclaw, Poland.ORCID 0000-0001-9077-439X
Michał OstrówkaFaculty of Biotechnology, University of Wroclaw, Fryderyka Joliot-Curie 14a, 50-137 Wroclaw, Poland.
Anna Duda-MadejDepartment of Microbiology, Faculty of Medicine, Wroclaw Medical University, Chalubinskiego 4, 50-368 Wroclaw, Poland.ORCID 0000-0001-8559-1695
Paweł MackiewiczFaculty of Biotechnology, University of Wroclaw, Fryderyka Joliot-Curie 14a, 50-137 Wroclaw, Poland.ORCID 0000-0003-4855-497X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antimicrobial peptides (AMPs) are emerging as a promising alternative to traditional antibiotics due to their ability to disturb bacterial membranes and/or their intracellular processes, offering a potential solution to the growing problem of antimicrobial resistance. AMP effectiveness is governed by factors such as net charge, hydrophobicity, and the ability to form amphipathic secondary structures. When properly balanced, these characteristics enable AMPs to selectively target bacterial membranes while sparing eukaryotic cells. This review focuses on the roles of positive charge, hydrophobicity, and structure in influencing AMP activity and toxicity, and explores strategies to optimize them for enhanced therapeutic potential. We highlight the delicate balance between these properties and how various modifications, including amino acid substitutions, peptide tagging, or lipid conjugation, can either enhance or impair AMP performance. Notably, an increase in these parameters does not always yield the best results; sometimes, a slight reduction in charge, hydrophobicity, or structural stability improves the overall AMP therapeutic potential. Understanding these complex interactions is key to developing AMPs with greater antimicrobial activity and reduced toxicity, making them viable candidates in the fight against antibiotic-resistant bacteria.

Indexed as

Hydrophobic and Hydrophilic InteractionsAnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesAntimicrobial PeptidesBacteriaHumansStructure-Activity RelationshipAnti-Bacterial AgentsAntimicrobial Cationic PeptidesAntimicrobial Peptidesantimicrobial peptidesantimicrobial resistancecationic peptideschargehydrophobicitypeptide optimizationsynthetic peptides

Identifiers

PMID39409150
PMCPMC11476776

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.