Self-assembly of platelet lysates proteins into microparticles by unnatural disulfide bonds for bottom-up tissue engineering

Detalhes bibliográficos
Autor(a) principal: Gomes, Maria C.
Data de Publicação: 2023
Outros Autores: Pinho, Ana Rita, Custódio, Catarina, Mano, João F.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10773/38540
Resumo: There is a demand to design microparticles holding surface topographies while presenting inherent bioactive cues for applications in the biomedical and biotechnological fields. Using the pool of proteins present in human-derived platelet lysates (PL), it is reported the production of protein-based microparticles via a simple and cost-effective method, exploring the prone redox behavior of cysteine (-SH) amino acid residues. The forced formation of new intermolecular disulfide bonds results in the precipitation of the proteins as spherical, pompon-like microparticles with adjustable sizes (15-50 μm in diameter) and surface topography consisting of grooves and ridges. These PL microparticles exhibit extraordinary cytocompatibility, allowing cell-guided micro-aggregates to form, while also working as injectable systems for cell support. Early studies also suggests that the surface topography provided by these PL microparticles can support osteogenic behavior. Consequently, these PL microparticles may find use to create live tissues via bottom-up procedures or injectable tissue-defect fillers, particularly for bone regeneration, with the prospect of working under xeno-free conditions.
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spelling Self-assembly of platelet lysates proteins into microparticles by unnatural disulfide bonds for bottom-up tissue engineeringPool of proteinsProtein-based microparticlesSurface topographiesMicro-carriersInjectable systems3D constructsThere is a demand to design microparticles holding surface topographies while presenting inherent bioactive cues for applications in the biomedical and biotechnological fields. Using the pool of proteins present in human-derived platelet lysates (PL), it is reported the production of protein-based microparticles via a simple and cost-effective method, exploring the prone redox behavior of cysteine (-SH) amino acid residues. The forced formation of new intermolecular disulfide bonds results in the precipitation of the proteins as spherical, pompon-like microparticles with adjustable sizes (15-50 μm in diameter) and surface topography consisting of grooves and ridges. These PL microparticles exhibit extraordinary cytocompatibility, allowing cell-guided micro-aggregates to form, while also working as injectable systems for cell support. Early studies also suggests that the surface topography provided by these PL microparticles can support osteogenic behavior. Consequently, these PL microparticles may find use to create live tissues via bottom-up procedures or injectable tissue-defect fillers, particularly for bone regeneration, with the prospect of working under xeno-free conditions.Wiley2024-06-24T00:00:00Z2023-06-24T00:00:00Z2023-06-24info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10773/38540eng0935-964810.1002/adma.202304659Gomes, Maria C.Pinho, Ana RitaCustódio, CatarinaMano, João F.info:eu-repo/semantics/embargoedAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-02-22T12:15:10Zoai:ria.ua.pt:10773/38540Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:08:56.394331Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Self-assembly of platelet lysates proteins into microparticles by unnatural disulfide bonds for bottom-up tissue engineering
title Self-assembly of platelet lysates proteins into microparticles by unnatural disulfide bonds for bottom-up tissue engineering
spellingShingle Self-assembly of platelet lysates proteins into microparticles by unnatural disulfide bonds for bottom-up tissue engineering
Gomes, Maria C.
Pool of proteins
Protein-based microparticles
Surface topographies
Micro-carriers
Injectable systems
3D constructs
title_short Self-assembly of platelet lysates proteins into microparticles by unnatural disulfide bonds for bottom-up tissue engineering
title_full Self-assembly of platelet lysates proteins into microparticles by unnatural disulfide bonds for bottom-up tissue engineering
title_fullStr Self-assembly of platelet lysates proteins into microparticles by unnatural disulfide bonds for bottom-up tissue engineering
title_full_unstemmed Self-assembly of platelet lysates proteins into microparticles by unnatural disulfide bonds for bottom-up tissue engineering
title_sort Self-assembly of platelet lysates proteins into microparticles by unnatural disulfide bonds for bottom-up tissue engineering
author Gomes, Maria C.
author_facet Gomes, Maria C.
Pinho, Ana Rita
Custódio, Catarina
Mano, João F.
author_role author
author2 Pinho, Ana Rita
Custódio, Catarina
Mano, João F.
author2_role author
author
author
dc.contributor.author.fl_str_mv Gomes, Maria C.
Pinho, Ana Rita
Custódio, Catarina
Mano, João F.
dc.subject.por.fl_str_mv Pool of proteins
Protein-based microparticles
Surface topographies
Micro-carriers
Injectable systems
3D constructs
topic Pool of proteins
Protein-based microparticles
Surface topographies
Micro-carriers
Injectable systems
3D constructs
description There is a demand to design microparticles holding surface topographies while presenting inherent bioactive cues for applications in the biomedical and biotechnological fields. Using the pool of proteins present in human-derived platelet lysates (PL), it is reported the production of protein-based microparticles via a simple and cost-effective method, exploring the prone redox behavior of cysteine (-SH) amino acid residues. The forced formation of new intermolecular disulfide bonds results in the precipitation of the proteins as spherical, pompon-like microparticles with adjustable sizes (15-50 μm in diameter) and surface topography consisting of grooves and ridges. These PL microparticles exhibit extraordinary cytocompatibility, allowing cell-guided micro-aggregates to form, while also working as injectable systems for cell support. Early studies also suggests that the surface topography provided by these PL microparticles can support osteogenic behavior. Consequently, these PL microparticles may find use to create live tissues via bottom-up procedures or injectable tissue-defect fillers, particularly for bone regeneration, with the prospect of working under xeno-free conditions.
publishDate 2023
dc.date.none.fl_str_mv 2023-06-24T00:00:00Z
2023-06-24
2024-06-24T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10773/38540
url http://hdl.handle.net/10773/38540
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0935-9648
10.1002/adma.202304659
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dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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