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Tyrosinase-Mediated Conjugation for Antigen Display on Ferritin Nanoparticles

2024-09-27Artigo científico Acesso aberto
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dc.contributor.authorRodrigues, Margarida Q.
dc.contributor.authorPatão, Sara
dc.contributor.authorThomaz, Mónica
dc.contributor.authorNunes, Tiago
dc.contributor.authorAlves, Paula M.
dc.contributor.authorRoldão, António
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.pblACS - American Chemical Society
dc.date.accessioned2025-05-07T21:25:39Z
dc.date.available2025-05-07T21:25:39Z
dc.date.issued2024-09-27
dc.descriptionFunding Information: The authors acknowledge the support from European Commission (Project PROMETEUS, grant number 823780) and Portuguese Fundac\u0327a\u0303o para a Cie\u0302ncia e a Tecnologia (FCT) through the following programs: FCT Investigator Starting Grant (IF/01704/2014), Exploratory Research and Development Project (EXPL/BBB-BIO/1541/2013), and Ph.D. fellowship (DFA/BD/8167/2020). iNOVA4Health (UIDB/04462/2020 and UIDP/04462/2020) and the Associate Laboratory LS4FUTURE (LA/P/0087/2020), programs financially supported by FCT/Ministe\u0301rio da Cie\u0302ncia, Tecnologia e Ensino Superior through national funds, are acknowledged. Publisher Copyright: © 2024 The Authors. Published by American Chemical Society.
dc.description.abstractFerritin (Ft) nanoparticles have become versatile platforms for displaying antigens, being a promising technology for vaccine development. While genetic fusion has traditionally been the preferred method for antigen display, concerns about improper folding and steric hindrance that may compromise vaccine efficacy or stability have prompted alternative approaches. Bioconjugation offers the advantage of preserving native protein structure and function, with recent advancements improving efficiency and specificity. In this study, we used tyrosinase (TYR) to bioconjugate the receptor binding domain of the SARS-CoV-2 spike protein, tagged with a tyrosine (RBD-Y), to native cysteines on Ft, resulting in RBD-Y-Ft nanoparticles. We quantified available cysteines on ferritin using Ellman’s assay and monitored their reduction during the reactions. Denaturing analytics (via SDS-PAGE, Western blot, and LC-TOF-MS) confirmed the formation of RBD-Y-Ft monomers with an expected molecular weight of 46 kDa. Mass photometry and HPLC estimated a molecular weight of RBD-Y-Ft nanoparticles of 680 kDa, which was higher than that of nonfunctionalized ferritin (480 kDa), indicating successful binding of up to eight RBD-Y antigens per 24-mer Ft nanoparticle. This work enhances our understanding of how Ft nanoparticles can be engineered to present antigens, leveraging them as a robust scaffold for producing tailored-made candidate vaccines in a timely manner.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent4664861
dc.identifier.doi10.1021/acs.bioconjchem.4c00387
dc.identifier.issn1043-1802
dc.identifier.otherPURE: 112673237
dc.identifier.otherPURE UUID: 3bb7ba04-c243-4279-91ea-c461a82719e2
dc.identifier.otherScopus: 85205938779
dc.identifier.otherPubMed: 39332819
dc.identifier.urihttp://hdl.handle.net/10362/182795
dc.identifier.urlhttps://www.scopus.com/pages/publications/85205938779
dc.language.isoeng
dc.peerreviewedyes
dc.subjectBiotechnology
dc.subjectBioengineering
dc.subjectBiomedical Engineering
dc.subjectPharmacology
dc.subjectPharmaceutical Science
dc.subjectOrganic Chemistry
dc.subjectSDG 3 - Good Health and Well-being
dc.titleTyrosinase-Mediated Conjugation for Antigen Display on Ferritin Nanoparticlesen
dc.typejournal article
degois.publication.titleBioconjugate Chemistry
dspace.entity.typePublication
rcaap.rightsopenAccess

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