RQ18 Peptide Exerts Anti-Melanoma Effects via Apoptosis Induction.
6 affiliations
- 1Programa de Pós-Graduação em Bioquímica e Biologia Molecular, Instituto de Biociências (INBIO), Universidade Federal de Mato Grosso do Sul, Campo Grande 79070-900, MS, Brazil.
- 2Laboratório de Purificação de Proteínas e suas Funções Biológicas (LPPFB), Faculdade de Ciências Farmacêuticas, Alimentos e Nutrição (FACFAN), Universidade Federal de Mato Grosso do Sul, Campo Grande 79070-900, MS, Brazil.
- 3S-Inova Biotech, Programa de Pós-Graduação em Biotecnologia, Universidade Católica Dom Bosco, Campo Grande 79117-900, MS, Brazil.
- 4Centro de Estudos em Células Tronco, Terapia Celular e Genética Toxicológica (CeTroGen), Faculdade de Medicina (FAMED), Universidade Federal de Mato Grosso do Sul, Campo Grande 79070-900, MS, Brazil.
- 5Centro de Análises Proteômicas e Bioquímicas, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia, Universidade Católica de Brasília, Brasília 71966-700, DF, Brazil.
- 6Programa de Pós-Graduação em Ciências Ambientais e Sustentabilidade Agropecuária, Universidade Católica Dom Bosco, Campo Grande 79117-900, MS, Brazil.
Abstract
Background/Objectives: The rise in cancer cases is a major global public health problem. Treating the disease and maintaining health generate high economic and social costs. In recent years, treatment resistance has become a challenge, reinforcing the need for new anticancer agents. In this context, anticancer peptides (ACPs) stand out for their selective interaction with cancer cell membranes. This study aimed to evaluate the activity of the RQ18 peptide against cancer cells. Methods: The cytotoxicity of RQ18 was determined by the MTT assay in murine melanoma (B16F10-Nex2), human melanoma (Sk-mel-28 and A375), breast cancer (MCF-7), cervical cancer (HeLa), murine macrophage (RAW 264.7), and human fibroblast (FN1). Caspase-3/7 activity was further evaluated in B16F10-Nex2, Sk-mel-28, and A375 melanoma cells to investigate the involvement of apoptotic pathways. In addition, intracellular oxidative stress was assessed using the DCFH-DA probe in these three melanoma cell lines. In B16F10-Nex2 cells, cellular morphological changes were examined by microscopy, while apoptosis-associated events were characterized using the markers MitoTracker Deep Red, and NucBlue, complemented by flow cytometry analyses. In addition, molecular dynamics simulations were employed to investigate its interactions with lipid membranes. Results: The peptide exhibited anticancer activity, with IC₅₀ values of 4.4, 11.58 and 59.99 µM·mL⁻¹, against cells B16F10-Nex2, Sk-mel-28 and A375, respectively. Compared with non-cancerous cells, RQ18 preferentially affected cancer cells, especially B16F10-Nex2. In contrast, the peptide was nontoxic to healthy cells, thus indicating selectivity for cancer cells. Morphological analysis revealed alterations compatible with apoptosis, including cell rounding and chromatin condensation. RQ18 increased caspase-3/7 activity in B16F10-Nex2, Sk-mel-28, and A375 cells and induced intracellular oxidative stress, as indicated by increased DCFH-DA fluorescence. Flow cytometry data confirmed the induction of apoptotic cell death in B16F10-Nex2 cells. Caspase activation, detected by a caspase-3/7 assay in three melanoma cell lines, together with flow cytometry data, supported the involvement of apoptotic cell death. Molecular dynamics simulations suggest that the peptide interacts stably with cancer cell-like membranes and retains an α-helical conformation during membrane association. Conclusions: In summary, the RQ18 peptide demonstrates preferential anticancer activity, particularly against melanoma cells, supporting further investigation of its therapeutic potential.
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BibTeX
@article{almeida2026rq18,
title = {{RQ18 Peptide Exerts Anti-Melanoma Effects via Apoptosis Induction.}},
author = {Claudiane Vilharroel Almeida and Ana Cristina Jacobowski and Caio Fernando Ramalho de Oliveira and Luís Henrique de Oliveira Almeida and Camila de Oliveira Gutierrez and Tamaeh Monteiro-Alfredo and Lucas Rodrigues de Lima and Thais de Andrade Farias Rodrigues and Rodrigo Juliano Oliveira and Octávio Luiz Franco and Marlon Henrique Cardoso and Ana Paula de Araújo Boleti and Maria Lígia Rodrigues Macedo},
journal = {Pharmaceuticals (Basel, Switzerland)},
year = {2026},
month = sep,
doi = {10.3390/ph19101521},
url = {https://europepmc.org/article/MED/42943218},
note = {CC BY},
}
RIS
TY - JOUR
TI - RQ18 Peptide Exerts Anti-Melanoma Effects via Apoptosis Induction.
AU - Claudiane Vilharroel Almeida
AU - Ana Cristina Jacobowski
AU - Caio Fernando Ramalho de Oliveira
AU - Luís Henrique de Oliveira Almeida
AU - Camila de Oliveira Gutierrez
AU - Tamaeh Monteiro-Alfredo
AU - Lucas Rodrigues de Lima
AU - Thais de Andrade Farias Rodrigues
AU - Rodrigo Juliano Oliveira
AU - Octávio Luiz Franco
AU - Marlon Henrique Cardoso
AU - Ana Paula de Araújo Boleti
AU - Maria Lígia Rodrigues Macedo
PY - 2026
DA - 2026/09/25
JO - Pharmaceuticals (Basel, Switzerland)
DO - 10.3390/ph19101521
UR - https://europepmc.org/article/MED/42943218
AB - Background/Objectives: The rise in cancer cases is a major global public health problem. Treating the disease and maintaining health generate high economic and social costs. In recent years, treatment resistance has become a challenge, reinforcing the need for new anticancer agents. In this context, anticancer peptides (ACPs) stand out for their selective interaction with cancer cell membranes. This study aimed to evaluate the activity of the RQ18 peptide against cancer cells. Methods: The cytotoxicity of RQ18 was determined by the MTT assay in murine melanoma (B16F10-Nex2), human melanoma (Sk-mel-28 and A375), breast cancer (MCF-7), cervical cancer (HeLa), murine macrophage (RAW 264.7), and human fibroblast (FN1). Caspase-3/7 activity was further evaluated in B16F10-Nex2, Sk-mel-28, and A375 melanoma cells to investigate the involvement of apoptotic pathways. In addition, intracellular oxidative stress was assessed using the DCFH-DA probe in these three melanoma cell lines. In B16F10-Nex2 cells, cellular morphological changes were examined by microscopy, while apoptosis-associated events were characterized using the markers MitoTracker Deep Red, and NucBlue, complemented by flow cytometry analyses. In addition, molecular dynamics simulations were employed to investigate its interactions with lipid membranes. Results: The peptide exhibited anticancer activity, with IC₅₀ values of 4.4, 11.58 and 59.99 µM·mL⁻¹, against cells B16F10-Nex2, Sk-mel-28 and A375, respectively. Compared with non-cancerous cells, RQ18 preferentially affected cancer cells, especially B16F10-Nex2. In contrast, the peptide was nontoxic to healthy cells, thus indicating selectivity for cancer cells. Morphological analysis revealed alterations compatible with apoptosis, including cell rounding and chromatin condensation. RQ18 increased caspase-3/7 activity in B16F10-Nex2, Sk-mel-28, and A375 cells and induced intracellular oxidative stress, as indicated by increased DCFH-DA fluorescence. Flow cytometry data confirmed the induction of apoptotic cell death in B16F10-Nex2 cells. Caspase activation, detected by a caspase-3/7 assay in three melanoma cell lines, together with flow cytometry data, supported the involvement of apoptotic cell death. Molecular dynamics simulations suggest that the peptide interacts stably with cancer cell-like membranes and retains an α-helical conformation during membrane association. Conclusions: In summary, the RQ18 peptide demonstrates preferential anticancer activity, particularly against melanoma cells, supporting further investigation of its therapeutic potential.
SN - 1424-8247
ER -