Effect of surfactant protein A on the physical properties and surface activity of KL4-surfactant

SP-A, the major protein component of pulmonary surfactant, is absent in exogenous surfactants currently used in clinical practice. However, it is thought that therapeutic properties of natural surfactants improve after enrichment with SP-A. The objective of this study was to determine SP-A effects o...

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Detalhes bibliográficos
Autores: Sáenz, Alejandra, Cañadas Benito, Olga, Bagatolli, Luís, Sánchez Barbero, Fernando, Johnson, Mark, Casals Carro, María Cristina
Tipo de documento: artigo
Data de publicação:2007
País:España
Recursos:Universidad Complutense de Madrid (UCM)
Repositório:Docta Complutense
Idioma:inglês
OAI Identifier:oai:docta.ucm.es:20.500.14352/93174
Acesso em linha:https://hdl.handle.net/20.500.14352/93174
Access Level:Acceso aberto
Palavra-chave:577.112
612.2
Bioquímica (Biología)
Fisiología
2302 Bioquímica
2411.17 Fisiología de la Respiración
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spelling Effect of surfactant protein A on the physical properties and surface activity of KL4-surfactantSáenz, AlejandraCañadas Benito, OlgaBagatolli, LuísSánchez Barbero, FernandoJohnson, MarkCasals Carro, María Cristina577.112612.2Bioquímica (Biología)Fisiología2302 Bioquímica2411.17 Fisiología de la RespiraciónSP-A, the major protein component of pulmonary surfactant, is absent in exogenous surfactants currently used in clinical practice. However, it is thought that therapeutic properties of natural surfactants improve after enrichment with SP-A. The objective of this study was to determine SP-A effects on physical properties and surface activity of a new synthetic lung surfactant based on a cationic and hydrophobic 21-residue peptide KLLLLKLLLLKLLLLKLLLLK, KL4. We have analyzed the interaction of SP-A with liposomes consisting of DPPC/POPG/PA (28:9:5.6, w/w/w) with and without 0.57 mol % KL4 peptide. We found that SP-A had a concentration-dependent effect on the surface activity of KL4-DPPC/POPG/PA membranes but not on that of an animal-derived LES. The surface activity of KL4-surfactant significantly improved after enrichment with 2.5–5 wt % SP-A. However, it worsened at SP-A concentrations $10 wt %. This was due to the fluidizing effect of supraphysiological SP-A concentrations on KL4-DPPC/POPG/PA membranes as determined by fluorescence anisotropy measurements, calorimetric studies, and confocal fluorescence microscopy of GUVs. High SP-A concentrations caused disappearance of the solid/fluid phase coexistence of KL4-surfactant, suggesting that phase coexistence might be important for the surface adsorption process.ElsevierUniversidad Complutense de Madrid20072007-01-0120072007-01-01journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/93174reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/931742026-06-02T12:44:21Z
dc.title.none.fl_str_mv Effect of surfactant protein A on the physical properties and surface activity of KL4-surfactant
title Effect of surfactant protein A on the physical properties and surface activity of KL4-surfactant
spellingShingle Effect of surfactant protein A on the physical properties and surface activity of KL4-surfactant
Sáenz, Alejandra
577.112
612.2
Bioquímica (Biología)
Fisiología
2302 Bioquímica
2411.17 Fisiología de la Respiración
title_short Effect of surfactant protein A on the physical properties and surface activity of KL4-surfactant
title_full Effect of surfactant protein A on the physical properties and surface activity of KL4-surfactant
title_fullStr Effect of surfactant protein A on the physical properties and surface activity of KL4-surfactant
title_full_unstemmed Effect of surfactant protein A on the physical properties and surface activity of KL4-surfactant
title_sort Effect of surfactant protein A on the physical properties and surface activity of KL4-surfactant
dc.creator.none.fl_str_mv Sáenz, Alejandra
Cañadas Benito, Olga
Bagatolli, Luís
Sánchez Barbero, Fernando
Johnson, Mark
Casals Carro, María Cristina
author Sáenz, Alejandra
author_facet Sáenz, Alejandra
Cañadas Benito, Olga
Bagatolli, Luís
Sánchez Barbero, Fernando
Johnson, Mark
Casals Carro, María Cristina
author_role author
author2 Cañadas Benito, Olga
Bagatolli, Luís
Sánchez Barbero, Fernando
Johnson, Mark
Casals Carro, María Cristina
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv 577.112
612.2
Bioquímica (Biología)
Fisiología
2302 Bioquímica
2411.17 Fisiología de la Respiración
topic 577.112
612.2
Bioquímica (Biología)
Fisiología
2302 Bioquímica
2411.17 Fisiología de la Respiración
description SP-A, the major protein component of pulmonary surfactant, is absent in exogenous surfactants currently used in clinical practice. However, it is thought that therapeutic properties of natural surfactants improve after enrichment with SP-A. The objective of this study was to determine SP-A effects on physical properties and surface activity of a new synthetic lung surfactant based on a cationic and hydrophobic 21-residue peptide KLLLLKLLLLKLLLLKLLLLK, KL4. We have analyzed the interaction of SP-A with liposomes consisting of DPPC/POPG/PA (28:9:5.6, w/w/w) with and without 0.57 mol % KL4 peptide. We found that SP-A had a concentration-dependent effect on the surface activity of KL4-DPPC/POPG/PA membranes but not on that of an animal-derived LES. The surface activity of KL4-surfactant significantly improved after enrichment with 2.5–5 wt % SP-A. However, it worsened at SP-A concentrations $10 wt %. This was due to the fluidizing effect of supraphysiological SP-A concentrations on KL4-DPPC/POPG/PA membranes as determined by fluorescence anisotropy measurements, calorimetric studies, and confocal fluorescence microscopy of GUVs. High SP-A concentrations caused disappearance of the solid/fluid phase coexistence of KL4-surfactant, suggesting that phase coexistence might be important for the surface adsorption process.
publishDate 2007
dc.date.none.fl_str_mv 2007
2007-01-01
2007
2007-01-01
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/20.500.14352/93174
url https://hdl.handle.net/20.500.14352/93174
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
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:Docta Complutense
instname:Universidad Complutense de Madrid (UCM)
instname_str Universidad Complutense de Madrid (UCM)
reponame_str Docta Complutense
collection Docta Complutense
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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