Staphylococcus epidermidis RP62A adhesion to chemically modified cellulose derivatives

Detalhes bibliográficos
Autor(a) principal: Fonseca, A. P.
Data de Publicação: 2001
Outros Autores: Granja, P. L., Nogueira, J. A., Oliveira, Rosário, Barbosa, M. A.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/1718
Resumo: The adhesion of coagulase negative Staphylococcus epidermidis expressing capsular polysaccharide/adhesin (PS/A) to cellulose diacetate (CDA), as well as to primary reference low-density polyethylene, was assessed in vitro. Attached bacteria were released by gentle sonication and quantified as colony forming units. Surface free energy of cells and materials and the free energy of interaction between cells, each type of material and water molecules was calculated through contact angle measurement, also enabling the determination of materials surface hydrophobicity. The influence of CDA surface modification by deacetylation and phosphorylation on bacterial adhesion was studied. Chemical modifications of CDA by deacetylation and by phosphorylation were effective in lowering bacterial adhesion.
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spelling Staphylococcus epidermidis RP62A adhesion to chemically modified cellulose derivativesScience & TechnologyThe adhesion of coagulase negative Staphylococcus epidermidis expressing capsular polysaccharide/adhesin (PS/A) to cellulose diacetate (CDA), as well as to primary reference low-density polyethylene, was assessed in vitro. Attached bacteria were released by gentle sonication and quantified as colony forming units. Surface free energy of cells and materials and the free energy of interaction between cells, each type of material and water molecules was calculated through contact angle measurement, also enabling the determination of materials surface hydrophobicity. The influence of CDA surface modification by deacetylation and phosphorylation on bacterial adhesion was studied. Chemical modifications of CDA by deacetylation and by phosphorylation were effective in lowering bacterial adhesion.KluwerUniversidade do MinhoFonseca, A. P.Granja, P. L.Nogueira, J. A.Oliveira, RosárioBarbosa, M. A.20012001-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/1718eng“Journal of material science. Materials in medicine”. 12 (2001) 543-548.0957-453010.1023/A:1011227915575info: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:RCAAP2023-07-21T11:53:51Zoai:repositorium.sdum.uminho.pt:1822/1718Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:43:19.319733Repositório 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 Staphylococcus epidermidis RP62A adhesion to chemically modified cellulose derivatives
title Staphylococcus epidermidis RP62A adhesion to chemically modified cellulose derivatives
spellingShingle Staphylococcus epidermidis RP62A adhesion to chemically modified cellulose derivatives
Fonseca, A. P.
Science & Technology
title_short Staphylococcus epidermidis RP62A adhesion to chemically modified cellulose derivatives
title_full Staphylococcus epidermidis RP62A adhesion to chemically modified cellulose derivatives
title_fullStr Staphylococcus epidermidis RP62A adhesion to chemically modified cellulose derivatives
title_full_unstemmed Staphylococcus epidermidis RP62A adhesion to chemically modified cellulose derivatives
title_sort Staphylococcus epidermidis RP62A adhesion to chemically modified cellulose derivatives
author Fonseca, A. P.
author_facet Fonseca, A. P.
Granja, P. L.
Nogueira, J. A.
Oliveira, Rosário
Barbosa, M. A.
author_role author
author2 Granja, P. L.
Nogueira, J. A.
Oliveira, Rosário
Barbosa, M. A.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Fonseca, A. P.
Granja, P. L.
Nogueira, J. A.
Oliveira, Rosário
Barbosa, M. A.
dc.subject.por.fl_str_mv Science & Technology
topic Science & Technology
description The adhesion of coagulase negative Staphylococcus epidermidis expressing capsular polysaccharide/adhesin (PS/A) to cellulose diacetate (CDA), as well as to primary reference low-density polyethylene, was assessed in vitro. Attached bacteria were released by gentle sonication and quantified as colony forming units. Surface free energy of cells and materials and the free energy of interaction between cells, each type of material and water molecules was calculated through contact angle measurement, also enabling the determination of materials surface hydrophobicity. The influence of CDA surface modification by deacetylation and phosphorylation on bacterial adhesion was studied. Chemical modifications of CDA by deacetylation and by phosphorylation were effective in lowering bacterial adhesion.
publishDate 2001
dc.date.none.fl_str_mv 2001
2001-01-01T00:00:00Z
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/1822/1718
url http://hdl.handle.net/1822/1718
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv “Journal of material science. Materials in medicine”. 12 (2001) 543-548.
0957-4530
10.1023/A:1011227915575
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 Kluwer
publisher.none.fl_str_mv Kluwer
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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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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