Evidence map›Paper›PMID 41210724›Full record

ArticleACS omega2025

A Lactoferricin B/Buforin Chimeric Peptide Causes a Rapid, Selective, Prolonged Cytotoxic Effect and Induces Apoptosis in HPV18-Positive Cervical Cancer Cells.

Natalia Ardila-Chantré, Andrea Carolina Barragán-Cárdenas, Juan Esteban Reyes-Calderón, Dennis Santiago Franco-Zambrano, Edwar Alejandro Matta-Orjuela, Jhon Erick Rivera-Monroy, Emma Muñoz-Sáez, Claudia Carabaña-García, Claudia Marcela Parra-Giraldo, Ricardo Fierro-Medina and 2 more

Abstract read
In one paragraph

Article in ACS omega, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

12 authors.

Natalia Ardila-ChantréDepartamento de Farmacia, Facultad de Ciencias, Universidad Nacional de ColombiaSede Bogotá, Carrera 45 No 26-85, Building 450, Bogotá 11321, Colombia.
Andrea Carolina Barragán-CárdenasUniversidad Colegio Mayor de Cundinamarca, Calle 28 No. 5B-02, Bogotá 110311, Colombia.
Juan Esteban Reyes-CalderónDepartamento de Química, Facultad de Ciencias, Universidad Nacional de ColombiaSede Bogotá, Carrera 45 No 26-85, Building 451, Bogotá 11321, Colombia.ORCID https://orcid.org/0000-0003-4734-3310
Dennis Santiago Franco-ZambranoDepartamento de Química, Facultad de Ciencias, Universidad Nacional de ColombiaSede Bogotá, Carrera 45 No 26-85, Building 451, Bogotá 11321, Colombia.
Edwar Alejandro Matta-OrjuelaDepartamento de Química, Facultad de Ciencias, Universidad Nacional de ColombiaSede Bogotá, Carrera 45 No 26-85, Building 451, Bogotá 11321, Colombia.
Jhon Erick Rivera-MonroyLaboratorio Instrumental de Alta Complejidad, Universidad de La Salle, Carrera 5 No. 59A-44, Bogotá 110231, Colombia.ORCID https://orcid.org/0000-0002-6911-9988
Emma Muñoz-SáezDepartamento de Biociencias, Universidad Europea, Calle Tajo, 28670 Villaviciosa de Odón, Madrid 28670, Spain.ORCID https://orcid.org/0000-0003-3654-0343
Claudia Carabaña-GarcíaDepartamento de Biociencias, Universidad Europea, Calle Tajo, 28670 Villaviciosa de Odón, Madrid 28670, Spain.
Claudia Marcela Parra-GiraldoDepartamento de Biociencias, Universidad Europea, Calle Tajo, 28670 Villaviciosa de Odón, Madrid 28670, Spain.
Ricardo Fierro-MedinaDepartamento de Química, Facultad de Ciencias, Universidad Nacional de ColombiaSede Bogotá, Carrera 45 No 26-85, Building 451, Bogotá 11321, Colombia.
Zuly Jenny Rivera-MonroyDepartamento de Química, Facultad de Ciencias, Universidad Nacional de ColombiaSede Bogotá, Carrera 45 No 26-85, Building 451, Bogotá 11321, Colombia.ORCID https://orcid.org/0000-0001-6915-8488
Javier Eduardo García-CastañedaDepartamento de Farmacia, Facultad de Ciencias, Universidad Nacional de ColombiaSede Bogotá, Carrera 45 No 26-85, Building 450, Bogotá 11321, Colombia.ORCID https://orcid.org/0000-0001-6882-4397

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study focuses on the chimeric peptide KKWQWK-Ahx-RLLRRLLR and its interaction with cancer cells, specifically HPV18-positive cervical cancer HeLa and Ca Ski cells. The main objective of this study was to understand the mode of action of this chimera related to its cytotoxic activity, as well as the internalization processes and the type of cell death induced. For this purpose, several in vitro and in vivo assays were performed, showing that the uptake of the chimera is not energy-dependent and could involve a passive transport process. The results suggested that chimera internalization can be mediated by a specific interaction of the peptide with molecules on the cell membrane. The cytotoxic effect of the chimera in cervical cancer cells causes severe morphological changes, including rounding, shrinking, and vacuole formation. It was also determined that the chimera primarily induces early and late apoptosis in HeLa cells, without causing necrosis, and activates caspases 3 and 7. The chimera was localized in both the cytoplasm and the nucleus of the cancer cells, suggesting that the peptide could interact with intracellular targets. In conclusion, this study provides a broader understanding of the mechanism of action of the KKWQWK-Ahx-RLLRRLLR chimera on cancer cells, highlighting its ability to induce a fast, selective, and significantly cytotoxic effect in cervical cancer cells, which involves cell death through the apoptotic pathway. The toxicity assays in

Identifiers

PMID41210724
PMCPMC12593040

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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.