Quantifying molecular partition of cellpenetrating peptide–cargo supramolecular complexes into lipid membranes : optimizing peptide-based drug delivery systems

Detalhes bibliográficos
Autor(a) principal: Freire, João Miguel
Data de Publicação: 2013
Outros Autores: Veiga, Ana Salomé, de la Torre, Beatriz G., Andreu, David, Castanho, Miguel A. R. B.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10451/10707
Resumo: Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.
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spelling Quantifying molecular partition of cellpenetrating peptide–cargo supramolecular complexes into lipid membranes : optimizing peptide-based drug delivery systemsDrug deliveryCell penetrating peptideMembrane interactionSpectroscopyFluorescenceCopyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.One of the major challenges in the drug development process is biodistribution across epithelia and intracellular drug targeting. Cellular membrane heterogeneity is one of the major drawbacks in developing efficient and sustainable drug delivery systems, which brings the need to study their interaction with lipids in order to unravel their mechanisms of action and improve their delivery capacities. Cell penetrating peptides (CPPs) are able to translocate almost any cell membrane carrying cargo molecules. However, different CPP use different entry mechanisms, which are often concentration-dependent and cargo-dependent. Being able to quantify the lipid affinity of CPP is of obvious importance and can be achieved by studying the partition extent of CPP into lipid bilayers. The partition constant (Kp) reflects the lipid–water partition extent. However, all currently available methodologies are only suitable to determine the partition of single molecules into lipid membranes or entities, being unsuitable to determine the partition of bimolecular or higher order supramolecular complexes. We derived and tested a mathematical model to determine the Kp of supramolecular CPP-cargo complexes from fluorescence spectroscopy data, using DNA oligomers as a model cargo. As a proof-of-concept example, the partition extent of two new membrane active peptides derived from dengue virus capsid protein (DENV C protein) with potential CPP properties, in both scenarios (free peptide and complexed with a molecular cargo), were tested. We were able to identify the lipid affinity of these CPP:DNA complexes, thus gaining valuable insights into better CPP formulations.This work was supported by projects PTDC/QUI/69937/2006 and PTDC/QUI-BIQ/112929/2009 from Fundação para a Ciência e Tecnologia – Ministério da Educação e Ciência (FCT-MEC, Portugal). JMF also acknowledges FCT-MEC for PhD fellowship SFRH/BD/70423/2010.WileyRepositório da Universidade de LisboaFreire, João MiguelVeiga, Ana Saloméde la Torre, Beatriz G.Andreu, DavidCastanho, Miguel A. R. B.2014-03-10T12:21:37Z20132013-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10451/10707engJ. Pept. Sci. 2013; 19: 182–1891075-2617http://dx.doi.org/10.1002/psc.2477metadata only accessinfo: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:RCAAP2024-11-20T17:14:40Zoai:repositorio.ul.pt:10451/10707Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-11-20T17:14:40Repositório 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 Quantifying molecular partition of cellpenetrating peptide–cargo supramolecular complexes into lipid membranes : optimizing peptide-based drug delivery systems
title Quantifying molecular partition of cellpenetrating peptide–cargo supramolecular complexes into lipid membranes : optimizing peptide-based drug delivery systems
spellingShingle Quantifying molecular partition of cellpenetrating peptide–cargo supramolecular complexes into lipid membranes : optimizing peptide-based drug delivery systems
Freire, João Miguel
Drug delivery
Cell penetrating peptide
Membrane interaction
Spectroscopy
Fluorescence
title_short Quantifying molecular partition of cellpenetrating peptide–cargo supramolecular complexes into lipid membranes : optimizing peptide-based drug delivery systems
title_full Quantifying molecular partition of cellpenetrating peptide–cargo supramolecular complexes into lipid membranes : optimizing peptide-based drug delivery systems
title_fullStr Quantifying molecular partition of cellpenetrating peptide–cargo supramolecular complexes into lipid membranes : optimizing peptide-based drug delivery systems
title_full_unstemmed Quantifying molecular partition of cellpenetrating peptide–cargo supramolecular complexes into lipid membranes : optimizing peptide-based drug delivery systems
title_sort Quantifying molecular partition of cellpenetrating peptide–cargo supramolecular complexes into lipid membranes : optimizing peptide-based drug delivery systems
author Freire, João Miguel
author_facet Freire, João Miguel
Veiga, Ana Salomé
de la Torre, Beatriz G.
Andreu, David
Castanho, Miguel A. R. B.
author_role author
author2 Veiga, Ana Salomé
de la Torre, Beatriz G.
Andreu, David
Castanho, Miguel A. R. B.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Repositório da Universidade de Lisboa
dc.contributor.author.fl_str_mv Freire, João Miguel
Veiga, Ana Salomé
de la Torre, Beatriz G.
Andreu, David
Castanho, Miguel A. R. B.
dc.subject.por.fl_str_mv Drug delivery
Cell penetrating peptide
Membrane interaction
Spectroscopy
Fluorescence
topic Drug delivery
Cell penetrating peptide
Membrane interaction
Spectroscopy
Fluorescence
description Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.
publishDate 2013
dc.date.none.fl_str_mv 2013
2013-01-01T00:00:00Z
2014-03-10T12:21:37Z
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/10451/10707
url http://hdl.handle.net/10451/10707
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv J. Pept. Sci. 2013; 19: 182–189
1075-2617
http://dx.doi.org/10.1002/psc.2477
dc.rights.driver.fl_str_mv metadata only access
info:eu-repo/semantics/openAccess
rights_invalid_str_mv metadata only access
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
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
repository.mail.fl_str_mv mluisa.alvim@gmail.com
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