Ohmic heating as a new tool for protein scaffold engineering
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/1822/70470 |
Resumo: | Ohmic heating (OH) is recognised as an emerging processing technology which recently is gaining increasing attention due to its ability to induce and control protein functionality. In this study, OH was used for the first time in the production of scaffolds for tissue engineering. BSA/casein solutions were processed by OH, promoting protein denaturation and aggregation, followed by cold-gelation through the addition of Ca2+. The formation of stable scaffolds was mostly dependent on the temperature and treatment time during OH processing. The variations of the electric field (EF) induced changes in the functional properties of both gel forming solutions and final scaffolds (contact angle, swelling, porosity, compressive modulus and degradation rate). The scaffolds biological performance was evaluated regarding their ability to support the adhesion and proliferation of human fibroblast cells. The production process resulted in a non-cytotoxic material and the changes imposed by the presence of the EF during the scaffolds production improved cellular proliferation and metabolic activity. Protein functionalization assisted by OH presents a promising new alternative for the production of improved and tuneable protein-based scaffolds for tissue engineering. |
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Ohmic heating as a new tool for protein scaffold engineeringgelationscaffoldselectric filedtissue engineeringcell proliferationScience & TechnologyOhmic heating (OH) is recognised as an emerging processing technology which recently is gaining increasing attention due to its ability to induce and control protein functionality. In this study, OH was used for the first time in the production of scaffolds for tissue engineering. BSA/casein solutions were processed by OH, promoting protein denaturation and aggregation, followed by cold-gelation through the addition of Ca2+. The formation of stable scaffolds was mostly dependent on the temperature and treatment time during OH processing. The variations of the electric field (EF) induced changes in the functional properties of both gel forming solutions and final scaffolds (contact angle, swelling, porosity, compressive modulus and degradation rate). The scaffolds biological performance was evaluated regarding their ability to support the adhesion and proliferation of human fibroblast cells. The production process resulted in a non-cytotoxic material and the changes imposed by the presence of the EF during the scaffolds production improved cellular proliferation and metabolic activity. Protein functionalization assisted by OH presents a promising new alternative for the production of improved and tuneable protein-based scaffolds for tissue engineering.This study was supported by the Portuguese Foundation for Science and Technology (FCT) under the scope of the strategic funding of UIDB/04469/2020 unit and BioTecNorte operation (NORTE-01-0145-FEDER000004) funded by the European Regional Development Fund under the scope of Norte2020 - Programa Operacional Regional do Norte.info:eu-repo/semantics/publishedVersionElsevierUniversidade do MinhoRodrigues, Rui Miguel MartinsPereira, Ricardo Nuno CorreiaVicente, A. A.Cavaco-Paulo, ArturRibeiro, Artur20212021-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/70470engRodrigues, Rui M.; Pereira, Ricardo N.; Vicente, António A.; Cavaco-Paulo, Artur; Ribeiro, Artur, Ohmic heating as a new tool for protein scaffold engineering. Materials Science and Engineering C-Materials for Biological Applications, 120(111784), 20210928-493110.1016/j.msec.2020.11178433545911111784https://www.sciencedirect.com/science/article/abs/pii/S0928493120337036info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-21T12:42:28Zoai:repositorium.sdum.uminho.pt:1822/70470Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:39:42.976587Repositório 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 |
Ohmic heating as a new tool for protein scaffold engineering |
title |
Ohmic heating as a new tool for protein scaffold engineering |
spellingShingle |
Ohmic heating as a new tool for protein scaffold engineering Rodrigues, Rui Miguel Martins gelation scaffolds electric filed tissue engineering cell proliferation Science & Technology |
title_short |
Ohmic heating as a new tool for protein scaffold engineering |
title_full |
Ohmic heating as a new tool for protein scaffold engineering |
title_fullStr |
Ohmic heating as a new tool for protein scaffold engineering |
title_full_unstemmed |
Ohmic heating as a new tool for protein scaffold engineering |
title_sort |
Ohmic heating as a new tool for protein scaffold engineering |
author |
Rodrigues, Rui Miguel Martins |
author_facet |
Rodrigues, Rui Miguel Martins Pereira, Ricardo Nuno Correia Vicente, A. A. Cavaco-Paulo, Artur Ribeiro, Artur |
author_role |
author |
author2 |
Pereira, Ricardo Nuno Correia Vicente, A. A. Cavaco-Paulo, Artur Ribeiro, Artur |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Rodrigues, Rui Miguel Martins Pereira, Ricardo Nuno Correia Vicente, A. A. Cavaco-Paulo, Artur Ribeiro, Artur |
dc.subject.por.fl_str_mv |
gelation scaffolds electric filed tissue engineering cell proliferation Science & Technology |
topic |
gelation scaffolds electric filed tissue engineering cell proliferation Science & Technology |
description |
Ohmic heating (OH) is recognised as an emerging processing technology which recently is gaining increasing attention due to its ability to induce and control protein functionality. In this study, OH was used for the first time in the production of scaffolds for tissue engineering. BSA/casein solutions were processed by OH, promoting protein denaturation and aggregation, followed by cold-gelation through the addition of Ca2+. The formation of stable scaffolds was mostly dependent on the temperature and treatment time during OH processing. The variations of the electric field (EF) induced changes in the functional properties of both gel forming solutions and final scaffolds (contact angle, swelling, porosity, compressive modulus and degradation rate). The scaffolds biological performance was evaluated regarding their ability to support the adhesion and proliferation of human fibroblast cells. The production process resulted in a non-cytotoxic material and the changes imposed by the presence of the EF during the scaffolds production improved cellular proliferation and metabolic activity. Protein functionalization assisted by OH presents a promising new alternative for the production of improved and tuneable protein-based scaffolds for tissue engineering. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021 2021-01-01T00:00:00Z |
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/1822/70470 |
url |
http://hdl.handle.net/1822/70470 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Rodrigues, Rui M.; Pereira, Ricardo N.; Vicente, António A.; Cavaco-Paulo, Artur; Ribeiro, Artur, Ohmic heating as a new tool for protein scaffold engineering. Materials Science and Engineering C-Materials for Biological Applications, 120(111784), 2021 0928-4931 10.1016/j.msec.2020.111784 33545911 111784 https://www.sciencedirect.com/science/article/abs/pii/S0928493120337036 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
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 |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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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 |
repository.mail.fl_str_mv |
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1799132939413356544 |