RQ18 Peptide Exerts Anti-Melanoma Effects via Apoptosis Induction

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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Journal
Pharmaceuticals
Published
2026-09-25
DOI
https://doi.org/10.3390/ph19101521
Primary Topic
Antimicrobial Peptides and Activities
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article
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article

RQ18 Peptide Exerts Anti-Melanoma Effects via Apoptosis Induction

Tamaeh Monteiro‐Alfredo, Octávio Luiz Franco, Ana Cristina Jacobowski, Claudiane Vilharroel Almeida et al.
Pharmaceuticals
Antimicrobial Peptides and Activities
article

RQ18 Peptide Exerts Anti-Melanoma Effects via Apoptosis Induction

Tamaeh Monteiro‐Alfredo, Octávio Luiz Franco, Ana Cristina Jacobowski, Claudiane Vilharroel Almeida, Luís Henrique de Oliveira Almeida, Marlon Henrique e Silva Cardoso, Lucas Rodrigues de Lima, Rodrigo Juliano Oliveira, Maria Lı́gia Rodrigues Macedo, Thaís de Andrade Farias Rodrigues, Caio Fernando Ramalho de Oliveira, Camila de Oliveira Gutierrez, Ana Paula de Araújo Boleti
article en

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.

PharmaceuticalsVol. 19(10)
Universidade Federal de Mato Grosso do Sul (BR), Universidade Católica de Brasília (BR), Universidade Católica Dom Bosco (BR)
Openalex Percentile: Top 14%
Antimicrobial Peptides and Activities
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