Improving the affinity of fibroblasts for bacterial cellulose using carbohydrate-binding modules fused to RGD
Autor(a) principal: | |
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Data de Publicação: | 2010 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | https://hdl.handle.net/1822/10230 |
Resumo: | The attachment of cells to biomedical materials can be improved by using adhesion sequences, such as Arg-Gly-Asp (RGD), found in several extracellular matrix proteins. In this work, bifunctional recombinant proteins, with a Cellulose-Binding Module (CBM), from the cellulosome of Clostridium thermocellum and cell binding sequences - RGD, GRGDY - were cloned and expressed in E.coli. These RGD-containing cellulose binding proteins were purified and used to coat bacterial cellulose fibres. Its effect on the cell adhesion/biocompatibility properties was tested using a mouse embryo fibroblasts culture. Bacterial cellulose (BC) secreted by Gluconacetobacter xylinus (=Acetobacter xylinum) is a material with unique properties and promising biomedical applications. CBMs adsorbs specifically and tightly on cellulose. Thus, they are a useful tool to address the fused RGD sequence (or other bioactive peptides) to the cellulose surface, in a specific and simple way. Indeed, fibroblasts exhibit improved ability to interact with bacterial cellulose sheets coated with RGD-CBM proteins, as compared with cellulose treated with the CBM, that is, without the adhesion peptide. The effect of the several fusion proteins produced was analyzed. |
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Improving the affinity of fibroblasts for bacterial cellulose using carbohydrate-binding modules fused to RGDBacterial celluloseCBMFibroblastsRGDCell adhesionCBM, fibroblastsScience & TechnologyThe attachment of cells to biomedical materials can be improved by using adhesion sequences, such as Arg-Gly-Asp (RGD), found in several extracellular matrix proteins. In this work, bifunctional recombinant proteins, with a Cellulose-Binding Module (CBM), from the cellulosome of Clostridium thermocellum and cell binding sequences - RGD, GRGDY - were cloned and expressed in E.coli. These RGD-containing cellulose binding proteins were purified and used to coat bacterial cellulose fibres. Its effect on the cell adhesion/biocompatibility properties was tested using a mouse embryo fibroblasts culture. Bacterial cellulose (BC) secreted by Gluconacetobacter xylinus (=Acetobacter xylinum) is a material with unique properties and promising biomedical applications. CBMs adsorbs specifically and tightly on cellulose. Thus, they are a useful tool to address the fused RGD sequence (or other bioactive peptides) to the cellulose surface, in a specific and simple way. Indeed, fibroblasts exhibit improved ability to interact with bacterial cellulose sheets coated with RGD-CBM proteins, as compared with cellulose treated with the CBM, that is, without the adhesion peptide. The effect of the several fusion proteins produced was analyzed.Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES, Brazil)Fundação para a Ciência e a Tecnologia (FCT)John Wiley and SonsUniversidade do MinhoAndrade, Fábia K.Moreira, Susana Margarida GomesDomingues, LucíliaGama, F. M.2010-012010-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/1822/10230eng"Journal of Biomedical Materials Research : Part A". ISSN 1549-3296. 92A:1 (Jan. 2010) 9-17.1549-329610.1002/jbm.a.3228419165790info: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:RCAAP2023-07-21T12:04:04Zoai:repositorium.sdum.uminho.pt:1822/10230Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:54:15.498497Repositório 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 |
Improving the affinity of fibroblasts for bacterial cellulose using carbohydrate-binding modules fused to RGD |
title |
Improving the affinity of fibroblasts for bacterial cellulose using carbohydrate-binding modules fused to RGD |
spellingShingle |
Improving the affinity of fibroblasts for bacterial cellulose using carbohydrate-binding modules fused to RGD Andrade, Fábia K. Bacterial cellulose CBM Fibroblasts RGD Cell adhesion CBM, fibroblasts Science & Technology |
title_short |
Improving the affinity of fibroblasts for bacterial cellulose using carbohydrate-binding modules fused to RGD |
title_full |
Improving the affinity of fibroblasts for bacterial cellulose using carbohydrate-binding modules fused to RGD |
title_fullStr |
Improving the affinity of fibroblasts for bacterial cellulose using carbohydrate-binding modules fused to RGD |
title_full_unstemmed |
Improving the affinity of fibroblasts for bacterial cellulose using carbohydrate-binding modules fused to RGD |
title_sort |
Improving the affinity of fibroblasts for bacterial cellulose using carbohydrate-binding modules fused to RGD |
author |
Andrade, Fábia K. |
author_facet |
Andrade, Fábia K. Moreira, Susana Margarida Gomes Domingues, Lucília Gama, F. M. |
author_role |
author |
author2 |
Moreira, Susana Margarida Gomes Domingues, Lucília Gama, F. M. |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Andrade, Fábia K. Moreira, Susana Margarida Gomes Domingues, Lucília Gama, F. M. |
dc.subject.por.fl_str_mv |
Bacterial cellulose CBM Fibroblasts RGD Cell adhesion CBM, fibroblasts Science & Technology |
topic |
Bacterial cellulose CBM Fibroblasts RGD Cell adhesion CBM, fibroblasts Science & Technology |
description |
The attachment of cells to biomedical materials can be improved by using adhesion sequences, such as Arg-Gly-Asp (RGD), found in several extracellular matrix proteins. In this work, bifunctional recombinant proteins, with a Cellulose-Binding Module (CBM), from the cellulosome of Clostridium thermocellum and cell binding sequences - RGD, GRGDY - were cloned and expressed in E.coli. These RGD-containing cellulose binding proteins were purified and used to coat bacterial cellulose fibres. Its effect on the cell adhesion/biocompatibility properties was tested using a mouse embryo fibroblasts culture. Bacterial cellulose (BC) secreted by Gluconacetobacter xylinus (=Acetobacter xylinum) is a material with unique properties and promising biomedical applications. CBMs adsorbs specifically and tightly on cellulose. Thus, they are a useful tool to address the fused RGD sequence (or other bioactive peptides) to the cellulose surface, in a specific and simple way. Indeed, fibroblasts exhibit improved ability to interact with bacterial cellulose sheets coated with RGD-CBM proteins, as compared with cellulose treated with the CBM, that is, without the adhesion peptide. The effect of the several fusion proteins produced was analyzed. |
publishDate |
2010 |
dc.date.none.fl_str_mv |
2010-01 2010-01-01T00:00:00Z |
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 |
https://hdl.handle.net/1822/10230 |
url |
https://hdl.handle.net/1822/10230 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
"Journal of Biomedical Materials Research : Part A". ISSN 1549-3296. 92A:1 (Jan. 2010) 9-17. 1549-3296 10.1002/jbm.a.32284 19165790 |
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 |
John Wiley and Sons |
publisher.none.fl_str_mv |
John Wiley and Sons |
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 |
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 |
repository.mail.fl_str_mv |
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1799132324773756928 |