Evidence of protein adsorption in pegylated liposomes: Influence of liposomal decoration

In order to contribute to a better knowledge of the events involved in the formation of the protein corona when nanoparticles (NPs) come in contact with proteins, we report a study about the changes on the physicochemical properties of pristine, PEGylated and Cyclic Arginine-Glycine-Aspartate peptid...

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Autores: Sangrà, Marc, Estelrich i Latràs, Joan, Sabaté Lagunas, Raimon, Espargaró Colomé, Alba, Busquets i Viñas, Ma. Antonia
Tipo de documento: artigo
Estado:Versão publicada
Data de publicação:2017
País:España
Recursos:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositório:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/108113
Acesso em linha:https://hdl.handle.net/2445/108113
Access Level:Acceso aberto
Palavra-chave:Liposomes
Proteïnes
Fluorescència
Nanopartícules
Proteins
Fluorescence
Nanoparticles
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spelling Evidence of protein adsorption in pegylated liposomes: Influence of liposomal decorationSangrà, MarcEstelrich i Latràs, JoanSabaté Lagunas, RaimonEspargaró Colomé, AlbaBusquets i Viñas, Ma. AntoniaLiposomesProteïnesFluorescènciaNanopartículesLiposomesProteinsFluorescenceNanoparticlesIn order to contribute to a better knowledge of the events involved in the formation of the protein corona when nanoparticles (NPs) come in contact with proteins, we report a study about the changes on the physicochemical properties of pristine, PEGylated and Cyclic Arginine-Glycine-Aspartate peptide (RGD)-functionalized large unilamelar liposomes (LUVs) or magnetoliposomes (MLs) upon incubation with Bovine Serum Albumin (BSA). The main phospholipid component of both LUVs and MLs was L-α-phosphatydylcholine (PC) or 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) with 20% of cholesterol. The most obvious indication of the interaction of BSA-nanosystems is given by changes in the hydrodynamic diameter of the particles but other evidence is needed to corroborate the process. Our findings indicate that size modification is a process that is accomplished in few hours and that is strongly dependent not only on the surface decoration but also of the lipid composition of both LUVs and MLs. Fluorescence quenching experiments as well as cryogenic transmission electron microscopy (Cryo-TEM) images assessed these changes and confirmed that although each system has to be studied in a particular way, we can establish three distinctive features that turn into more reactive systems: (a) compositions containing PC compared with their DMPC counterparts; (b) the presence of PEG and/or RGD compared to the pristine counterparts; and (c) the presence of SPIONs: MLs show higher interaction than LUVs of the same lipid composition. Consequently, PEGylation (that is supposed to make stealth NPs) actually fails in preventing complete protein binding.MDPI2017201720172017info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion16 p.application/pdfhttps://hdl.handle.net/2445/108113Articles publicats en revistes (Farmàcia, Tecnologia Farmacèutica i Fisicoquímica)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésReproducció del document publicat a: https://doi.org/10.3390/nano7020037Nanomaterials, 2017, vol. 7, num. 2, p. 37-52https://doi.org/10.3390/nano7020037cc-by (c) Sangrà, Marc et al., 2017http://creativecommons.org/licenses/by/3.0/esinfo:eu-repo/semantics/openAccessoai:recercat.cat:2445/1081132026-05-29T05:05:01Z
dc.title.none.fl_str_mv Evidence of protein adsorption in pegylated liposomes: Influence of liposomal decoration
title Evidence of protein adsorption in pegylated liposomes: Influence of liposomal decoration
spellingShingle Evidence of protein adsorption in pegylated liposomes: Influence of liposomal decoration
Sangrà, Marc
Liposomes
Proteïnes
Fluorescència
Nanopartícules
Liposomes
Proteins
Fluorescence
Nanoparticles
title_short Evidence of protein adsorption in pegylated liposomes: Influence of liposomal decoration
title_full Evidence of protein adsorption in pegylated liposomes: Influence of liposomal decoration
title_fullStr Evidence of protein adsorption in pegylated liposomes: Influence of liposomal decoration
title_full_unstemmed Evidence of protein adsorption in pegylated liposomes: Influence of liposomal decoration
title_sort Evidence of protein adsorption in pegylated liposomes: Influence of liposomal decoration
dc.creator.none.fl_str_mv Sangrà, Marc
Estelrich i Latràs, Joan
Sabaté Lagunas, Raimon
Espargaró Colomé, Alba
Busquets i Viñas, Ma. Antonia
author Sangrà, Marc
author_facet Sangrà, Marc
Estelrich i Latràs, Joan
Sabaté Lagunas, Raimon
Espargaró Colomé, Alba
Busquets i Viñas, Ma. Antonia
author_role author
author2 Estelrich i Latràs, Joan
Sabaté Lagunas, Raimon
Espargaró Colomé, Alba
Busquets i Viñas, Ma. Antonia
author2_role author
author
author
author
dc.subject.none.fl_str_mv Liposomes
Proteïnes
Fluorescència
Nanopartícules
Liposomes
Proteins
Fluorescence
Nanoparticles
topic Liposomes
Proteïnes
Fluorescència
Nanopartícules
Liposomes
Proteins
Fluorescence
Nanoparticles
description In order to contribute to a better knowledge of the events involved in the formation of the protein corona when nanoparticles (NPs) come in contact with proteins, we report a study about the changes on the physicochemical properties of pristine, PEGylated and Cyclic Arginine-Glycine-Aspartate peptide (RGD)-functionalized large unilamelar liposomes (LUVs) or magnetoliposomes (MLs) upon incubation with Bovine Serum Albumin (BSA). The main phospholipid component of both LUVs and MLs was L-α-phosphatydylcholine (PC) or 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) with 20% of cholesterol. The most obvious indication of the interaction of BSA-nanosystems is given by changes in the hydrodynamic diameter of the particles but other evidence is needed to corroborate the process. Our findings indicate that size modification is a process that is accomplished in few hours and that is strongly dependent not only on the surface decoration but also of the lipid composition of both LUVs and MLs. Fluorescence quenching experiments as well as cryogenic transmission electron microscopy (Cryo-TEM) images assessed these changes and confirmed that although each system has to be studied in a particular way, we can establish three distinctive features that turn into more reactive systems: (a) compositions containing PC compared with their DMPC counterparts; (b) the presence of PEG and/or RGD compared to the pristine counterparts; and (c) the presence of SPIONs: MLs show higher interaction than LUVs of the same lipid composition. Consequently, PEGylation (that is supposed to make stealth NPs) actually fails in preventing complete protein binding.
publishDate 2017
dc.date.none.fl_str_mv 2017
2017
2017
2017
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/108113
url https://hdl.handle.net/2445/108113
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.3390/nano7020037
Nanomaterials, 2017, vol. 7, num. 2, p. 37-52
https://doi.org/10.3390/nano7020037
dc.rights.none.fl_str_mv cc-by (c) Sangrà, Marc et al., 2017
http://creativecommons.org/licenses/by/3.0/es
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by (c) Sangrà, Marc et al., 2017
http://creativecommons.org/licenses/by/3.0/es
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 16 p.
application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv Articles publicats en revistes (Farmàcia, Tecnologia Farmacèutica i Fisicoquímica)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869417125302501376
score 15.812429

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