Evidence map›Paper›PMID 38854567›Full record

ArticleACS omega2024

Optimizing Bothropstoxin-I-Derived Peptides: Exploring the Antibacterial Potential of p-BthW.

Gabriela Marinho Righetto, Norival Alves Santos-Filho, Letícia Oliveira Catarin Nunes, Camille André, Julia Medeiros Souza, Adriano Defini Andricopulo, Paulo José Martins Bispo, Eduardo Maffud Cilli, Ilana Lopes Baratella da Cunha Camargo

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Article in ACS omega, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Gabriela Marinho RighettoLaboratory of Molecular Epidemiology and Microbiology, Department of Physics and Interdisciplinary Science, University of Sao Paulo, 13563-120 São Carlos, Brazil.ORCID https://orcid.org/0000-0002-7756-7545
Norival Alves Santos-FilhoDepartment of Biochemistry and Organic Chemistry, Institute of Chemistry, São Paulo State University, 14800-060 Araraquara, Brazil.
Letícia Oliveira Catarin NunesDepartment of Biochemistry and Organic Chemistry, Institute of Chemistry, São Paulo State University, 14800-060 Araraquara, Brazil.
Camille AndréInfectious Disease Institute, Department of Ophthalmology, Massachusetts Eye and Ear, Harvard Medical School, Boston, Massachusetts 02115, United States.
Julia Medeiros SouzaLaboratory of Medicinal and Computational Chemistry, Department of Physics and Interdisciplinary Science, University of Sao Paulo, 13563-120 São Carlos, Brazil.
Adriano Defini AndricopuloLaboratory of Medicinal and Computational Chemistry, Department of Physics and Interdisciplinary Science, University of Sao Paulo, 13563-120 São Carlos, Brazil.ORCID https://orcid.org/0000-0002-0457-818X
Paulo José Martins BispoInfectious Disease Institute, Department of Ophthalmology, Massachusetts Eye and Ear, Harvard Medical School, Boston, Massachusetts 02115, United States.
Eduardo Maffud CilliDepartment of Biochemistry and Organic Chemistry, Institute of Chemistry, São Paulo State University, 14800-060 Araraquara, Brazil.ORCID https://orcid.org/0000-0002-4767-0904
Ilana Lopes Baratella da Cunha CamargoLaboratory of Molecular Epidemiology and Microbiology, Department of Physics and Interdisciplinary Science, University of Sao Paulo, 13563-120 São Carlos, Brazil.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antimicrobial peptides are an emerging class of antibiotics that present a series of advantageous characteristics such as wide structural variety, broad spectrum of activity, and low propensity to select for resistance. They are found in all classes of life as defense molecules. A group of peptides derived from the protein Bothropstoxin-I has been previously studied as an alternative treatment against multi-drug-resistant bacteria. The peptide p-BthTX-I (sequence: KKYRYHLKPFCKK) and its homodimer, linked by disulfide oxidation through the residues of Cys11 and the serum degradation product [sequence: (KKYRYHLKPFC)

Identifiers

PMID38854567
PMCPMC11154919

What OpenQuestion holds

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Registered trials

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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.