Evidence map›Paper›PMID 33445476›Full record

ArticleMembranes2021

How Insertion of a Single Tryptophan in the N-Terminus of a Cecropin A-Melittin Hybrid Peptide Changes Its Antimicrobial and Biophysical Profile.

Ana Rita Ferreira, Cátia Teixeira, Carla F Sousa, Lucinda J Bessa, Paula Gomes, Paula Gameiro

Open access · goldAbstract read
In one paragraph

Article in Membranes, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Therapeutic Bioactivity Exerted by theMolecules (Basel, Switzerland) · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Deciphering the Mechanism of Action of the Antimicrobial Peptide BP100.International journal of molecular sciences · 2024
    Review
  11. Article
  12. Article
  13. Mechanisms of aPharmaceutics · 2023
    Article
  14. Article
  15. Stapling of Peptides Potentiates the Antibiotic Treatment ofAntibiotics (Basel, Switzerland) · 2022
    Article
  16. Article
  17. 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

6 authors at 1 institution in 2 countries.

Ana Rita FerreiraLaboratório Associado para a Química Verde da Rede de Química e Tecnologia (LAQV-REQUIMTE), Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, 4169-007 Porto, Portugal.
Cátia TeixeiraLaboratório Associado para a Química Verde da Rede de Química e Tecnologia (LAQV-REQUIMTE), Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, 4169-007 Porto, Portugal.ORCID 0000-0001-9506-3781
Carla F SousaLaboratório Associado para a Química Verde da Rede de Química e Tecnologia (LAQV-REQUIMTE), Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, 4169-007 Porto, Portugal.ORCID 0000-0002-6735-3455
Lucinda J BessaLaboratório Associado para a Química Verde da Rede de Química e Tecnologia (LAQV-REQUIMTE), Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, 4169-007 Porto, Portugal.ORCID 0000-0001-8339-1964
Paula GomesLaboratório Associado para a Química Verde da Rede de Química e Tecnologia (LAQV-REQUIMTE), Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, 4169-007 Porto, Portugal.ORCID 0000-0002-6018-4724
Paula GameiroLaboratório Associado para a Química Verde da Rede de Química e Tecnologia (LAQV-REQUIMTE), Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, 4169-007 Porto, Portugal.ORCID 0000-0002-4747-6853
Universidade do Porto · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the era of antibiotic resistance, there is an urgent need for efficient antibiotic therapies to fight bacterial infections. Cationic antimicrobial peptides (CAMP) are promising lead compounds given their membrane-targeted mechanism of action, and high affinity towards the anionic composition of bacterial membranes. We present a new CAMP, W-BP100, derived from the highly active BP100, holding an additional tryptophan at the N-terminus. W-BP100 showed a broader antibacterial activity, demonstrating a potent activity against Gram-positive strains. Revealing a high partition constant towards anionic over zwitterionic large unilamellar vesicles and inducing membrane saturation at a high peptide/lipid ratio, W-BP100 has a preferential location for hydrophobic environments. Contrary to BP100, almost no aggregation of anionic vesicles is observed around saturation conditions and at higher concentrations no aggregation is observed. With these results, it is possible to state that with the incorporation of a single tryptophan to the N-terminus, a highly active peptide was obtained due to the π-electron system of tryptophan, resulting in negatively charged clouds, that participate in cation-π interactions with lysine residues. Furthermore, we propose that W-BP100 action can be achieved by electrostatic interactions followed by peptide translocation.

Indexed as

antibiotic resistanceCAMPcation-π interactionscecropin-melittin peptideslarge unilamellar vesiclesmembrane-targeting activitytryptophan

Identifiers

PMID33445476
PMCPMC7826622
OpenAlexW3120148936

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.