AFM study of morphology and mechanical properties of a chimeric 2 spider silk and bone sialoprotein protein for bone regeneration

Detalhes bibliográficos
Autor(a) principal: Gomes, Sílvia C.
Data de Publicação: 2011
Outros Autores: Numata, Keiji, Leonor, I. B., Mano, J. F., Reis, R. L., Kaplan, David
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/12825
Resumo: Atomic force microscopy (AFM) was used to assess a new chimeric protein consisting of a fusion protein of the consensus repeat for Nephila clavipes spider dragline protein and bone sialoprotein (6merþBSP). The elastic modulus of this protein in film form was assessed through force curves, and film surface roughness was also determined. The results showed a significant difference among the elastic modulus of the chimeric silk protein, 6merþBSP, and control films consisting of only the silk component (6mer). The behavior of the 6merþBSP and 6mer proteins in aqueous solution in the presence of calcium (Ca) ions was also assessed to determine interactions between the inorganic and organic components related to bone interactions, anchoring, and biomaterial network formation. The results demonstrated the formation of protein networks in the presence of Ca2þ ions, characteristics that may be important in the context of controlling materials assembly and properties related to bone formation with this new chimeric silk-BSP protein.
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spelling AFM study of morphology and mechanical properties of a chimeric 2 spider silk and bone sialoprotein protein for bone regenerationAFMSilkScience & TechnologyAtomic force microscopy (AFM) was used to assess a new chimeric protein consisting of a fusion protein of the consensus repeat for Nephila clavipes spider dragline protein and bone sialoprotein (6merþBSP). The elastic modulus of this protein in film form was assessed through force curves, and film surface roughness was also determined. The results showed a significant difference among the elastic modulus of the chimeric silk protein, 6merþBSP, and control films consisting of only the silk component (6mer). The behavior of the 6merþBSP and 6mer proteins in aqueous solution in the presence of calcium (Ca) ions was also assessed to determine interactions between the inorganic and organic components related to bone interactions, anchoring, and biomaterial network formation. The results demonstrated the formation of protein networks in the presence of Ca2þ ions, characteristics that may be important in the context of controlling materials assembly and properties related to bone formation with this new chimeric silk-BSP protein.Silvia Games thanks the Foundation for Science and Technology (FCT) for supporting her Ph.D. grant, SFRH/BD/28603/2006. This work was carried out under the scope of the European NoE EXPERTISSUES (NMP3-CT-2004-500283), the Chimera project (PTDC/EBB-EBI/109093/2008) funded by the FCT agency, the NIH (P41 EB002520) Tissue Engineering Resource Center, and the NIH (EB003210 and DE017207).American Chemical SocietyUniversidade do MinhoGomes, Sílvia C.Numata, KeijiLeonor, I. B.Mano, J. F.Reis, R. L.Kaplan, David2011-052011-05-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/12825eng1525-779710.1021/bm200060521370930info: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:RCAAP2023-07-21T12:31:33Zoai:repositorium.sdum.uminho.pt:1822/12825Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:26:48.357998Repositório 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 AFM study of morphology and mechanical properties of a chimeric 2 spider silk and bone sialoprotein protein for bone regeneration
title AFM study of morphology and mechanical properties of a chimeric 2 spider silk and bone sialoprotein protein for bone regeneration
spellingShingle AFM study of morphology and mechanical properties of a chimeric 2 spider silk and bone sialoprotein protein for bone regeneration
Gomes, Sílvia C.
AFM
Silk
Science & Technology
title_short AFM study of morphology and mechanical properties of a chimeric 2 spider silk and bone sialoprotein protein for bone regeneration
title_full AFM study of morphology and mechanical properties of a chimeric 2 spider silk and bone sialoprotein protein for bone regeneration
title_fullStr AFM study of morphology and mechanical properties of a chimeric 2 spider silk and bone sialoprotein protein for bone regeneration
title_full_unstemmed AFM study of morphology and mechanical properties of a chimeric 2 spider silk and bone sialoprotein protein for bone regeneration
title_sort AFM study of morphology and mechanical properties of a chimeric 2 spider silk and bone sialoprotein protein for bone regeneration
author Gomes, Sílvia C.
author_facet Gomes, Sílvia C.
Numata, Keiji
Leonor, I. B.
Mano, J. F.
Reis, R. L.
Kaplan, David
author_role author
author2 Numata, Keiji
Leonor, I. B.
Mano, J. F.
Reis, R. L.
Kaplan, David
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Gomes, Sílvia C.
Numata, Keiji
Leonor, I. B.
Mano, J. F.
Reis, R. L.
Kaplan, David
dc.subject.por.fl_str_mv AFM
Silk
Science & Technology
topic AFM
Silk
Science & Technology
description Atomic force microscopy (AFM) was used to assess a new chimeric protein consisting of a fusion protein of the consensus repeat for Nephila clavipes spider dragline protein and bone sialoprotein (6merþBSP). The elastic modulus of this protein in film form was assessed through force curves, and film surface roughness was also determined. The results showed a significant difference among the elastic modulus of the chimeric silk protein, 6merþBSP, and control films consisting of only the silk component (6mer). The behavior of the 6merþBSP and 6mer proteins in aqueous solution in the presence of calcium (Ca) ions was also assessed to determine interactions between the inorganic and organic components related to bone interactions, anchoring, and biomaterial network formation. The results demonstrated the formation of protein networks in the presence of Ca2þ ions, characteristics that may be important in the context of controlling materials assembly and properties related to bone formation with this new chimeric silk-BSP protein.
publishDate 2011
dc.date.none.fl_str_mv 2011-05
2011-05-01T00:00:00Z
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/1822/12825
url http://hdl.handle.net/1822/12825
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1525-7797
10.1021/bm2000605
21370930
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 American Chemical Society
publisher.none.fl_str_mv American Chemical Society
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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