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A Biomimetic, Silaffin R5-Based Antigen Delivery Platform

Nature offers a wide range of evolutionary optimized materials that combine unique properties with intrinsic biocompatibility and that can be exploited as biomimetic materials. The R5 and RRIL peptides employed here are derived from silaffin proteins that play a crucial role in the biomineralization...

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Detalles Bibliográficos
Autores principales: Reichinger, Daniela, Reithofer, Manuel, Hohagen, Mariam, Drinic, Mirjana, Tobias, Joshua, Wiedermann, Ursula, Kleitz, Freddy, Jahn-Schmid, Beatrice, Becker, Christian F. W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9866965/
https://www.ncbi.nlm.nih.gov/pubmed/36678751
http://dx.doi.org/10.3390/pharmaceutics15010121
Descripción
Sumario:Nature offers a wide range of evolutionary optimized materials that combine unique properties with intrinsic biocompatibility and that can be exploited as biomimetic materials. The R5 and RRIL peptides employed here are derived from silaffin proteins that play a crucial role in the biomineralization of marine diatom silica shells and are also able to form silica materials in vitro. Here, we demonstrate the application of biomimetic silica particles as a vaccine delivery and adjuvant platform by linking the precipitating peptides R5 and the RRIL motif to a variety of peptide antigens. The resulting antigen-loaded silica particles combine the advantages of biomaterial-based vaccines with the proven intracellular uptake of silica particles. These particles induce NETosis in human neutrophils as well as IL-6 and TNF-α secretion in murine bone marrow-derived dendritic cells.