Rationally designed peptide induces apoptosis and cell cycle modulation in resistant melanoma

The ineffectiveness of conventional therapies against melanoma necessitates the development of novel approaches characterized by high selectivity and low systemic toxicity. Using computational optimization, KW18, a synthetic α-helical peptide, was rationally engineered. It incorporates conserved bio...

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Published in:Biochimica et biophysica acta. General subjects Vol. 1870; no. 1; p. 130877
Main Authors: Rocha, Layza Sá, Jacobowski, Ana Cristina, Thiburcio, Eduarda, Pereira, Rafael Araujo, Almeida, Claudiane Vilharroel, Gutierrez, Camila De Oliveira, de Andrade Farias Rodrigues, Thaís, Oliveira, Rodrigo Juliano, Taveira, Gabriel B., Hiane, Priscila Aiko, de Araújo Boleti, Ana Paula, Franco, Octávio Luiz, Cardoso, Marlon Henrique, Macedo, Maria Ligia Rodrigues
Format: Journal Article
Language:English
Published: Netherlands Elsevier B.V 01.01.2026
Subjects:
Anticancer peptide
Apoptosis
Computational design
Melanoma
Tumor-selective peptide
Tumor-selective peptide
Melanoma
Computational design
Anticancer peptide
Apoptosis
ISSN:0304-4165, 1872-8006, 1872-8006
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Abstract The ineffectiveness of conventional therapies against melanoma necessitates the development of novel approaches characterized by high selectivity and low systemic toxicity. Using computational optimization, KW18, a synthetic α-helical peptide, was rationally engineered. It incorporates conserved bioactive motifs from patented peptides. The Joker algorithm was used to refine the peptide. This process enhanced its positive charge, hydrophobicity, and α-helical stability. In vitro, KW18 displayed potent cytotoxicity against melanoma cells (IC₅₀ = 11.41–21.75 μM) with 84–91 % inhibition at 128 μM, minimal toxicity to FN1 fibroblasts, hemolysis below 5 %, and stability exceeding 80 %. Functional assays revealed mitochondrial damage and caspase-dependent apoptosis (86.5 % late apoptosis at 24 h). Cell cycle analysis in B16F10-Nex2 cells revealed a moderate accumulation in G0/G1 phase (62.9 %) alongside a substantial S-phase population (25.8 %), with minimal Sub-G0 (5.2 %) and reduced G2/M (6.1 %). This profile suggests a cytostatic-like effect through partial cell cycle slowdown. Structural characterization via helical wheel projections and circular dichroism confirmed its α-helical conformation, consistent with membrane-targeting activity. In vivo, Galleria mellonella larvae exposed to KW18 exhibited 100 % survival, supporting a favorable safety profile. Collectively, KW18 combines apoptosis induction with cell cycle modulation, offering a dual mechanism against melanoma while sparing healthy cells. These findings designate KW18 as a stable, selective, and safe therapeutic option for drug-resistant melanoma and a beneficial element for combined treatments. [Display omitted] •KW18 is a motif-based hybrid peptide rationally designed using bioinformatics.•Selectively cytotoxic to melanoma cells while sparing human fibroblasts.•Induces apoptosis (up to 86.5 %) through caspase-dependent mechanisms.•Modulates cell cycle by reducing G2/M and enriching S-phase population.•Shows low hemolysis and in vivo safety in Galleria mellonella model.
AbstractList The ineffectiveness of conventional therapies against melanoma necessitates the development of novel approaches characterized by high selectivity and low systemic toxicity. Using computational optimization, KW18, a synthetic α-helical peptide, was rationally engineered. It incorporates conserved bioactive motifs from patented peptides. The Joker algorithm was used to refine the peptide. This process enhanced its positive charge, hydrophobicity, and α-helical stability. In vitro, KW18 displayed potent cytotoxicity against melanoma cells (IC₅₀ = 11.41-21.75 μM) with 84-91 % inhibition at 128 μM, minimal toxicity to FN1 fibroblasts, hemolysis below 5 %, and stability exceeding 80 %. Functional assays revealed mitochondrial damage and caspase-dependent apoptosis (86.5 % late apoptosis at 24 h). Cell cycle analysis in B16F10-Nex2 cells revealed a moderate accumulation in G0/G1 phase (62.9 %) alongside a substantial S-phase population (25.8 %), with minimal Sub-G0 (5.2 %) and reduced G2/M (6.1 %). This profile suggests a cytostatic-like effect through partial cell cycle slowdown. Structural characterization via helical wheel projections and circular dichroism confirmed its α-helical conformation, consistent with membrane-targeting activity. In vivo, Galleria mellonella larvae exposed to KW18 exhibited 100 % survival, supporting a favorable safety profile. Collectively, KW18 combines apoptosis induction with cell cycle modulation, offering a dual mechanism against melanoma while sparing healthy cells. These findings designate KW18 as a stable, selective, and safe therapeutic option for drug-resistant melanoma and a beneficial element for combined treatments.
The ineffectiveness of conventional therapies against melanoma necessitates the development of novel approaches characterized by high selectivity and low systemic toxicity. Using computational optimization, KW18, a synthetic α-helical peptide, was rationally engineered. It incorporates conserved bioactive motifs from patented peptides. The Joker algorithm was used to refine the peptide. This process enhanced its positive charge, hydrophobicity, and α-helical stability. In vitro, KW18 displayed potent cytotoxicity against melanoma cells (IC₅₀ = 11.41-21.75 μM) with 84-91 % inhibition at 128 μM, minimal toxicity to FN1 fibroblasts, hemolysis below 5 %, and stability exceeding 80 %. Functional assays revealed mitochondrial damage and caspase-dependent apoptosis (86.5 % late apoptosis at 24 h). Cell cycle analysis in B16F10-Nex2 cells revealed a moderate accumulation in G0/G1 phase (62.9 %) alongside a substantial S-phase population (25.8 %), with minimal Sub-G0 (5.2 %) and reduced G2/M (6.1 %). This profile suggests a cytostatic-like effect through partial cell cycle slowdown. Structural characterization via helical wheel projections and circular dichroism confirmed its α-helical conformation, consistent with membrane-targeting activity. In vivo, Galleria mellonella larvae exposed to KW18 exhibited 100 % survival, supporting a favorable safety profile. Collectively, KW18 combines apoptosis induction with cell cycle modulation, offering a dual mechanism against melanoma while sparing healthy cells. These findings designate KW18 as a stable, selective, and safe therapeutic option for drug-resistant melanoma and a beneficial element for combined treatments.The ineffectiveness of conventional therapies against melanoma necessitates the development of novel approaches characterized by high selectivity and low systemic toxicity. Using computational optimization, KW18, a synthetic α-helical peptide, was rationally engineered. It incorporates conserved bioactive motifs from patented peptides. The Joker algorithm was used to refine the peptide. This process enhanced its positive charge, hydrophobicity, and α-helical stability. In vitro, KW18 displayed potent cytotoxicity against melanoma cells (IC₅₀ = 11.41-21.75 μM) with 84-91 % inhibition at 128 μM, minimal toxicity to FN1 fibroblasts, hemolysis below 5 %, and stability exceeding 80 %. Functional assays revealed mitochondrial damage and caspase-dependent apoptosis (86.5 % late apoptosis at 24 h). Cell cycle analysis in B16F10-Nex2 cells revealed a moderate accumulation in G0/G1 phase (62.9 %) alongside a substantial S-phase population (25.8 %), with minimal Sub-G0 (5.2 %) and reduced G2/M (6.1 %). This profile suggests a cytostatic-like effect through partial cell cycle slowdown. Structural characterization via helical wheel projections and circular dichroism confirmed its α-helical conformation, consistent with membrane-targeting activity. In vivo, Galleria mellonella larvae exposed to KW18 exhibited 100 % survival, supporting a favorable safety profile. Collectively, KW18 combines apoptosis induction with cell cycle modulation, offering a dual mechanism against melanoma while sparing healthy cells. These findings designate KW18 as a stable, selective, and safe therapeutic option for drug-resistant melanoma and a beneficial element for combined treatments.
The ineffectiveness of conventional therapies against melanoma necessitates the development of novel approaches characterized by high selectivity and low systemic toxicity. Using computational optimization, KW18, a synthetic α-helical peptide, was rationally engineered. It incorporates conserved bioactive motifs from patented peptides. The Joker algorithm was used to refine the peptide. This process enhanced its positive charge, hydrophobicity, and α-helical stability. In vitro, KW18 displayed potent cytotoxicity against melanoma cells (IC₅₀ = 11.41–21.75 μM) with 84–91 % inhibition at 128 μM, minimal toxicity to FN1 fibroblasts, hemolysis below 5 %, and stability exceeding 80 %. Functional assays revealed mitochondrial damage and caspase-dependent apoptosis (86.5 % late apoptosis at 24 h). Cell cycle analysis in B16F10-Nex2 cells revealed a moderate accumulation in G0/G1 phase (62.9 %) alongside a substantial S-phase population (25.8 %), with minimal Sub-G0 (5.2 %) and reduced G2/M (6.1 %). This profile suggests a cytostatic-like effect through partial cell cycle slowdown. Structural characterization via helical wheel projections and circular dichroism confirmed its α-helical conformation, consistent with membrane-targeting activity. In vivo, Galleria mellonella larvae exposed to KW18 exhibited 100 % survival, supporting a favorable safety profile. Collectively, KW18 combines apoptosis induction with cell cycle modulation, offering a dual mechanism against melanoma while sparing healthy cells. These findings designate KW18 as a stable, selective, and safe therapeutic option for drug-resistant melanoma and a beneficial element for combined treatments. [Display omitted] •KW18 is a motif-based hybrid peptide rationally designed using bioinformatics.•Selectively cytotoxic to melanoma cells while sparing human fibroblasts.•Induces apoptosis (up to 86.5 %) through caspase-dependent mechanisms.•Modulates cell cycle by reducing G2/M and enriching S-phase population.•Shows low hemolysis and in vivo safety in Galleria mellonella model.
ArticleNumber 130877
Author Hiane, Priscila Aiko
Rocha, Layza Sá
Cardoso, Marlon Henrique
Pereira, Rafael Araujo
Thiburcio, Eduarda
Gutierrez, Camila De Oliveira
Franco, Octávio Luiz
Jacobowski, Ana Cristina
de Andrade Farias Rodrigues, Thaís
Almeida, Claudiane Vilharroel
Oliveira, Rodrigo Juliano
Taveira, Gabriel B.
de Araújo Boleti, Ana Paula
Macedo, Maria Ligia Rodrigues
Author_xml – sequence: 1
  givenname: Layza Sá
  surname: Rocha
  fullname: Rocha, Layza Sá
  organization: Laboratório de Purificação de Proteínas e suas Funções Biológicas, Universidade Federal do Mato Grosso do Sul, 79070-900 Campo Grande, MS, Brazil
– sequence: 2
  givenname: Ana Cristina
  surname: Jacobowski
  fullname: Jacobowski, Ana Cristina
  organization: Laboratório de Purificação de Proteínas e suas Funções Biológicas, Universidade Federal do Mato Grosso do Sul, 79070-900 Campo Grande, MS, Brazil
– sequence: 3
  givenname: Eduarda
  surname: Thiburcio
  fullname: Thiburcio, Eduarda
  organization: Laboratório de Purificação de Proteínas e suas Funções Biológicas, Universidade Federal do Mato Grosso do Sul, 79070-900 Campo Grande, MS, Brazil
– sequence: 4
  givenname: Rafael Araujo
  surname: Pereira
  fullname: Pereira, Rafael Araujo
  organization: Laboratório de Purificação de Proteínas e suas Funções Biológicas, Universidade Federal do Mato Grosso do Sul, 79070-900 Campo Grande, MS, Brazil
– sequence: 5
  givenname: Claudiane Vilharroel
  surname: Almeida
  fullname: Almeida, Claudiane Vilharroel
  organization: Laboratório de Purificação de Proteínas e suas Funções Biológicas, Universidade Federal do Mato Grosso do Sul, 79070-900 Campo Grande, MS, Brazil
– sequence: 6
  givenname: Camila De Oliveira
  surname: Gutierrez
  fullname: Gutierrez, Camila De Oliveira
  organization: Laboratório de Purificação de Proteínas e suas Funções Biológicas, Universidade Federal do Mato Grosso do Sul, 79070-900 Campo Grande, MS, Brazil
– sequence: 7
  givenname: Thaís
  surname: de Andrade Farias Rodrigues
  fullname: de Andrade Farias Rodrigues, Thaís
  organization: Centro de Estudos em Células Tronco, Terapia Celular e Genética Toxicológica (CeTroGen), Faculdade de Medicina (FAMED), Universidade Federal de Mato Grosso do Sul (UFMS), Campo Grande, Mato Grosso do Sul, Brazil
– sequence: 8
  givenname: Rodrigo Juliano
  surname: Oliveira
  fullname: Oliveira, Rodrigo Juliano
  organization: Centro de Estudos em Células Tronco, Terapia Celular e Genética Toxicológica (CeTroGen), Faculdade de Medicina (FAMED), Universidade Federal de Mato Grosso do Sul (UFMS), Campo Grande, Mato Grosso do Sul, Brazil
– sequence: 9
  givenname: Gabriel B.
  surname: Taveira
  fullname: Taveira, Gabriel B.
  organization: Laboratório de Fisiologia e Bioquímica de Microrganismos, Universidade do Norte Fluminense, Campos dos Goytacazes, RJ, Brazil
– sequence: 10
  givenname: Priscila Aiko
  surname: Hiane
  fullname: Hiane, Priscila Aiko
  organization: Faculdade de Ciências Farmacêuticas, Alimentos e Nutrição, UFMS, Brazil
– sequence: 11
  givenname: Ana Paula
  surname: de Araújo Boleti
  fullname: de Araújo Boleti, Ana Paula
  organization: Laboratório de Purificação de Proteínas e suas Funções Biológicas, Universidade Federal do Mato Grosso do Sul, 79070-900 Campo Grande, MS, Brazil
– sequence: 12
  givenname: Octávio Luiz
  surname: Franco
  fullname: Franco, Octávio Luiz
  organization: Centro de Análises Proteômicas e Bioquímicas, Pós-Graduação em Ciências Genômicas e Biotecnologia, Universidade Católica de Brasília, Brasília, Brazil
– sequence: 13
  givenname: Marlon Henrique
  surname: Cardoso
  fullname: Cardoso, Marlon Henrique
  organization: S-Inova Biotech, Programa de Pós-Graduação em Biotecnologia, Universidade Católica Dom Bosco, Campo Grande, Brazil
– sequence: 14
  givenname: Maria Ligia Rodrigues
  surname: Macedo
  fullname: Macedo, Maria Ligia Rodrigues
  email: ligiamacedo18@gmail.com
  organization: Laboratório de Purificação de Proteínas e suas Funções Biológicas, Universidade Federal do Mato Grosso do Sul, 79070-900 Campo Grande, MS, Brazil
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Keywords Tumor-selective peptide
Melanoma
Computational design
Anticancer peptide
Apoptosis
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Snippet The ineffectiveness of conventional therapies against melanoma necessitates the development of novel approaches characterized by high selectivity and low...
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SubjectTerms Anticancer peptide
Apoptosis
Computational design
Melanoma
Tumor-selective peptide
Title Rationally designed peptide induces apoptosis and cell cycle modulation in resistant melanoma
URI https://dx.doi.org/10.1016/j.bbagen.2025.130877
https://www.ncbi.nlm.nih.gov/pubmed/41187845
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