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Physalia physalis-a source of bioactive collagen for the cosmetic industry

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Detalhes bibliográficos
Resumo:Collagen, the most abundant structural protein in animals, is fundamental for tissue integrity and regeneration. Conventional mammalian sources face limitations related to sustainability, safety, and ethical concerns, underscoring the need for alternative biomaterials. Marine organisms, particularly jellyfish, offer a promising eco-friendly collagen source. In this study, collagen and collagen-derived peptides were extracted from the cnidarian Physalia physalis and biochemically characterized. Circular dichroism demonstrated partial loss of triple-helix structure, while SDS-PAGE revealed type I collagen related -chains together with low-molecular-weight fragments. The hydrolyzed collagen fractions exhibited keratinocyte and fibroblast cytocompatibility and increased keratinocyte migration. Moreover, P. physalis-derived peptides modulated inflammatory cytokine release in lipopolysaccharide-stimulated macrophages reducing tumor necrosis factor (TNF)- by 38% and increasing interleukin (IL)-10 by 29%. Based on these results, a stable bioactive serum formulation incorporating P. physalis collagen peptides was developed. Overall, this work demonstrates that bioactive peptides from P. physalis possess immunomodulatory and regenerative potential and represent a promising new marine resource for cosmetic applications.
Autores principais:Fernandes, Raquel
Outros Autores:Oliveira, Cristiana; Sousa, Diana F.; Costa-Barbosa, Augusto; Sampaio, Paula; Reis, Luis; Fidalgo, Javier; Barros, Ana N.; Teixeira, J. A.; Botelho, Claudia
Assunto:Physalia physalis Collagen Collagen peptides Keratinocytes Cellular migration Inflammation
Ano:2026
País:Portugal
Tipo de documento:artigo
Tipo de acesso:acesso aberto
Instituição associada:Universidade do Minho
Idioma:inglês
Origem:RepositóriUM - Universidade do Minho
Descrição
Resumo:Collagen, the most abundant structural protein in animals, is fundamental for tissue integrity and regeneration. Conventional mammalian sources face limitations related to sustainability, safety, and ethical concerns, underscoring the need for alternative biomaterials. Marine organisms, particularly jellyfish, offer a promising eco-friendly collagen source. In this study, collagen and collagen-derived peptides were extracted from the cnidarian Physalia physalis and biochemically characterized. Circular dichroism demonstrated partial loss of triple-helix structure, while SDS-PAGE revealed type I collagen related -chains together with low-molecular-weight fragments. The hydrolyzed collagen fractions exhibited keratinocyte and fibroblast cytocompatibility and increased keratinocyte migration. Moreover, P. physalis-derived peptides modulated inflammatory cytokine release in lipopolysaccharide-stimulated macrophages reducing tumor necrosis factor (TNF)- by 38% and increasing interleukin (IL)-10 by 29%. Based on these results, a stable bioactive serum formulation incorporating P. physalis collagen peptides was developed. Overall, this work demonstrates that bioactive peptides from P. physalis possess immunomodulatory and regenerative potential and represent a promising new marine resource for cosmetic applications.

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