Physalia physalis—A Source of Bioactive Collagen for the Cosmetic Industry
Authors:
- Raquel FernandesRaquel Fernandes
- Cristiana OliveiraCristiana Oliveira
- Diana Ferreira-SousaDiana Ferreira-Sousa
- Augusto Costa-BarbosaAugusto Costa-Barbosa
- Paula SampaioPaula Sampaio
- Luis ReisLuis Reis
- Javier FidalgoJavier Fidalgo
- Ana N. BarrosAna N. Barros
- José A. TeixeiraJosé A. Teixeira
- Claudia BotelhoClaudia Botelho
Open Access
- 19 December 2025
- journal article
- research article
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 27 (1) , 33
Abstract
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 α-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)-α 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.Keywords
Funding Information
- Fundação para a Ciência e a Tecnologia (UIDB/04469/2020)
- LABBELS—Associate Laboratory in Biotechnology, Bioengineering and Microelectromechanical Systems (LA/P/0029/2020)
- EEA Grants (PT-INNOVATION-0096)
This publication has 77 references indexed in Scilit:
- Jellyfish collagen: A promising and sustainable marine biomaterial with emerging applications in food, cosmetics, and biomedical— A reviewApplied Food Research, 2025
- Jellyfish Rhizostoma pulmo collected off Goa Coast (India) as a rich source of tryptophan containing collagen and its enhanced antioxidant potentialJournal of Food Science and Technology, 2023
- Handbook of the Extracellular Matrix2023
- Sequence-dependent mechanics of collagen reflect its structural and functional organizationBiophysical Journal, 2021
- The wound healing potential of collagen peptides derived from the jellyfish Rhopilema esculentumChinese Journal of Traumatology, 2019
- Collagen and collagenolytic proteases: A reviewBiocatalysis and Agricultural Biotechnology, 2018
- Extracellular matrix structureAdvanced Drug Delivery Reviews, 2016
- Cell MigrationComprehensive Physiology, 2012
- Collagen types analysis and differentiation by FTIR spectroscopyAnalytical and Bioanalytical Chemistry, 2009
- Structure and conformation of intramolecularly cross-linked collagenColloids and Surfaces B: Biointerfaces, 2005