Protein adsorption to oligo (Ethylene Glycol) self assembled monolayers with amide linkage experiments with fibrinogen, heparinised plasma and serum
Autor(a) principal: | |
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Data de Publicação: | 2001 |
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/1822/14106 |
Resumo: | Low protein adsorption is believed advantageous for blood-contacting materials and ethylene glycols (EG)-based polymeric compounds are often attached to surfaces for this purpose. In the present study, the adsorption of brinogen, serum, and plasma were studied by ellipsometry on a series of well-de ned oligo(EG) terminated alkane-thiols self-assembled on gold. The layers were prepared with compounds of the general structure HS-(CH2)15-CONH-EGn, where n D 2, 4, and 6. Methoxy-terminated tri(EG) undecanethiol and hydroxyl-terminated hexadecanethiol self-assembled monolayers (SAMs) were used as references. The results clearly demonstrate that the adsorption depends on the experimental conditions with small amounts of brinogen adsorbing from a single protein solution, but larger amounts of proteins from serum and plasma. The adsorption of brinogen and blood plasma decreased with an increasing number of EG repeats and was temperature-dependent. Signi cantly less serum adsorbed to methoxy tri(EG) than to hexa(EG) and more proteins remained on the latter surface after incubation in a sodiumdodecyl sulfate (SDS) solution, indicating a looser protein binding to the methoxy-terminated surface. All surfaces adsorbed complement factor 3 (C3) from serum and plasma, although no surfacemediated complement activationwas observed. The present study points to the importance of a careful choice of the proteinmodel system before general statements regardingthe protein repellantproperties of potential surfaces can be made. |
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Protein adsorption to oligo (Ethylene Glycol) self assembled monolayers with amide linkage experiments with fibrinogen, heparinised plasma and serumSelf-assembled monolayersOligo(ethylene glycol)Protein adsorptionFibrinogenHeparinized plasmaSerumComplementLow protein adsorption is believed advantageous for blood-contacting materials and ethylene glycols (EG)-based polymeric compounds are often attached to surfaces for this purpose. In the present study, the adsorption of brinogen, serum, and plasma were studied by ellipsometry on a series of well-de ned oligo(EG) terminated alkane-thiols self-assembled on gold. The layers were prepared with compounds of the general structure HS-(CH2)15-CONH-EGn, where n D 2, 4, and 6. Methoxy-terminated tri(EG) undecanethiol and hydroxyl-terminated hexadecanethiol self-assembled monolayers (SAMs) were used as references. The results clearly demonstrate that the adsorption depends on the experimental conditions with small amounts of brinogen adsorbing from a single protein solution, but larger amounts of proteins from serum and plasma. The adsorption of brinogen and blood plasma decreased with an increasing number of EG repeats and was temperature-dependent. Signi cantly less serum adsorbed to methoxy tri(EG) than to hexa(EG) and more proteins remained on the latter surface after incubation in a sodiumdodecyl sulfate (SDS) solution, indicating a looser protein binding to the methoxy-terminated surface. All surfaces adsorbed complement factor 3 (C3) from serum and plasma, although no surfacemediated complement activationwas observed. The present study points to the importance of a careful choice of the proteinmodel system before general statements regardingthe protein repellantproperties of potential surfaces can be made.Universidade do MinhoBenesch, JohanSvedhem, S.Svensson, S. C.Valiokas, R.Liedberg, B.Tengvall, P.20012001-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/14106eng0920-5063info: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:RCAAP2023-07-21T12:08:08Zoai:repositorium.sdum.uminho.pt:1822/14106Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:59:19.638353Repositório 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 |
Protein adsorption to oligo (Ethylene Glycol) self assembled monolayers with amide linkage experiments with fibrinogen, heparinised plasma and serum |
title |
Protein adsorption to oligo (Ethylene Glycol) self assembled monolayers with amide linkage experiments with fibrinogen, heparinised plasma and serum |
spellingShingle |
Protein adsorption to oligo (Ethylene Glycol) self assembled monolayers with amide linkage experiments with fibrinogen, heparinised plasma and serum Benesch, Johan Self-assembled monolayers Oligo(ethylene glycol) Protein adsorption Fibrinogen Heparinized plasma Serum Complement |
title_short |
Protein adsorption to oligo (Ethylene Glycol) self assembled monolayers with amide linkage experiments with fibrinogen, heparinised plasma and serum |
title_full |
Protein adsorption to oligo (Ethylene Glycol) self assembled monolayers with amide linkage experiments with fibrinogen, heparinised plasma and serum |
title_fullStr |
Protein adsorption to oligo (Ethylene Glycol) self assembled monolayers with amide linkage experiments with fibrinogen, heparinised plasma and serum |
title_full_unstemmed |
Protein adsorption to oligo (Ethylene Glycol) self assembled monolayers with amide linkage experiments with fibrinogen, heparinised plasma and serum |
title_sort |
Protein adsorption to oligo (Ethylene Glycol) self assembled monolayers with amide linkage experiments with fibrinogen, heparinised plasma and serum |
author |
Benesch, Johan |
author_facet |
Benesch, Johan Svedhem, S. Svensson, S. C. Valiokas, R. Liedberg, B. Tengvall, P. |
author_role |
author |
author2 |
Svedhem, S. Svensson, S. C. Valiokas, R. Liedberg, B. Tengvall, P. |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Benesch, Johan Svedhem, S. Svensson, S. C. Valiokas, R. Liedberg, B. Tengvall, P. |
dc.subject.por.fl_str_mv |
Self-assembled monolayers Oligo(ethylene glycol) Protein adsorption Fibrinogen Heparinized plasma Serum Complement |
topic |
Self-assembled monolayers Oligo(ethylene glycol) Protein adsorption Fibrinogen Heparinized plasma Serum Complement |
description |
Low protein adsorption is believed advantageous for blood-contacting materials and ethylene glycols (EG)-based polymeric compounds are often attached to surfaces for this purpose. In the present study, the adsorption of brinogen, serum, and plasma were studied by ellipsometry on a series of well-de ned oligo(EG) terminated alkane-thiols self-assembled on gold. The layers were prepared with compounds of the general structure HS-(CH2)15-CONH-EGn, where n D 2, 4, and 6. Methoxy-terminated tri(EG) undecanethiol and hydroxyl-terminated hexadecanethiol self-assembled monolayers (SAMs) were used as references. The results clearly demonstrate that the adsorption depends on the experimental conditions with small amounts of brinogen adsorbing from a single protein solution, but larger amounts of proteins from serum and plasma. The adsorption of brinogen and blood plasma decreased with an increasing number of EG repeats and was temperature-dependent. Signi cantly less serum adsorbed to methoxy tri(EG) than to hexa(EG) and more proteins remained on the latter surface after incubation in a sodiumdodecyl sulfate (SDS) solution, indicating a looser protein binding to the methoxy-terminated surface. All surfaces adsorbed complement factor 3 (C3) from serum and plasma, although no surfacemediated complement activationwas observed. The present study points to the importance of a careful choice of the proteinmodel system before general statements regardingthe protein repellantproperties of potential surfaces can be made. |
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/1822/14106 |
url |
http://hdl.handle.net/1822/14106 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0920-5063 |
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.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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1799132384981942272 |