The activity of LE10 peptide on biological membranes using molecular dynamics, in vitro and in vivo studies

Detalhes bibliográficos
Autor(a) principal: Antunes, José Egipto Ferreira
Data de Publicação: 2013
Outros Autores: Azóia, Nuno G., Matamá, Maria Teresa, Gomes, Andreia, Paulo, Artur Cavaco
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/24352
Resumo: Cell-penetrating peptides (CPPs) and antimicrobial peptides (AMPs) are generally defined as small cationic peptides with the ability to interact with lipidic membranes, in a process driven by electrostatic and hydrophobic processes. The interaction with CPPs is known to lead to its translocation across the membrane, while with AMPs lead to membrane damage. Here we present one synthetic anionic peptide, LE10 (LELELELELELELELELELE), which strongly interacts with model membranes, showing properties of CPPs (translocation through lipidic membranes on a mechanism usually described for cationic CPPs) and AMPs (membrane disruption) in molecular dynamic studies, experimental studies with liposomes and mammalian cells in vitro. Based on the LE10 properties here demonstrated, small modifications in its structure could make it a very promising tool for drug delivery.
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spelling The activity of LE10 peptide on biological membranes using molecular dynamics, in vitro and in vivo studiesAntimicrobial peptidesCell-penetrating peptidesLiposome disruptionMembrane active peptidesMolecular dynamicsScience & TechnologyCell-penetrating peptides (CPPs) and antimicrobial peptides (AMPs) are generally defined as small cationic peptides with the ability to interact with lipidic membranes, in a process driven by electrostatic and hydrophobic processes. The interaction with CPPs is known to lead to its translocation across the membrane, while with AMPs lead to membrane damage. Here we present one synthetic anionic peptide, LE10 (LELELELELELELELELELE), which strongly interacts with model membranes, showing properties of CPPs (translocation through lipidic membranes on a mechanism usually described for cationic CPPs) and AMPs (membrane disruption) in molecular dynamic studies, experimental studies with liposomes and mammalian cells in vitro. Based on the LE10 properties here demonstrated, small modifications in its structure could make it a very promising tool for drug delivery.ElsevierElsevier BVUniversidade do MinhoAntunes, José Egipto FerreiraAzóia, Nuno G.Matamá, Maria TeresaGomes, AndreiaPaulo, Artur Cavaco20132013-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/24352eng0927-776510.1016/j.colsurfb.2013.01.05023434718info: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:RCAAP2023-07-21T11:56:45Zoai:repositorium.sdum.uminho.pt:1822/24352Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:46:25.147257Repositório 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 The activity of LE10 peptide on biological membranes using molecular dynamics, in vitro and in vivo studies
title The activity of LE10 peptide on biological membranes using molecular dynamics, in vitro and in vivo studies
spellingShingle The activity of LE10 peptide on biological membranes using molecular dynamics, in vitro and in vivo studies
Antunes, José Egipto Ferreira
Antimicrobial peptides
Cell-penetrating peptides
Liposome disruption
Membrane active peptides
Molecular dynamics
Science & Technology
title_short The activity of LE10 peptide on biological membranes using molecular dynamics, in vitro and in vivo studies
title_full The activity of LE10 peptide on biological membranes using molecular dynamics, in vitro and in vivo studies
title_fullStr The activity of LE10 peptide on biological membranes using molecular dynamics, in vitro and in vivo studies
title_full_unstemmed The activity of LE10 peptide on biological membranes using molecular dynamics, in vitro and in vivo studies
title_sort The activity of LE10 peptide on biological membranes using molecular dynamics, in vitro and in vivo studies
author Antunes, José Egipto Ferreira
author_facet Antunes, José Egipto Ferreira
Azóia, Nuno G.
Matamá, Maria Teresa
Gomes, Andreia
Paulo, Artur Cavaco
author_role author
author2 Azóia, Nuno G.
Matamá, Maria Teresa
Gomes, Andreia
Paulo, Artur Cavaco
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Antunes, José Egipto Ferreira
Azóia, Nuno G.
Matamá, Maria Teresa
Gomes, Andreia
Paulo, Artur Cavaco
dc.subject.por.fl_str_mv Antimicrobial peptides
Cell-penetrating peptides
Liposome disruption
Membrane active peptides
Molecular dynamics
Science & Technology
topic Antimicrobial peptides
Cell-penetrating peptides
Liposome disruption
Membrane active peptides
Molecular dynamics
Science & Technology
description Cell-penetrating peptides (CPPs) and antimicrobial peptides (AMPs) are generally defined as small cationic peptides with the ability to interact with lipidic membranes, in a process driven by electrostatic and hydrophobic processes. The interaction with CPPs is known to lead to its translocation across the membrane, while with AMPs lead to membrane damage. Here we present one synthetic anionic peptide, LE10 (LELELELELELELELELELE), which strongly interacts with model membranes, showing properties of CPPs (translocation through lipidic membranes on a mechanism usually described for cationic CPPs) and AMPs (membrane disruption) in molecular dynamic studies, experimental studies with liposomes and mammalian cells in vitro. Based on the LE10 properties here demonstrated, small modifications in its structure could make it a very promising tool for drug delivery.
publishDate 2013
dc.date.none.fl_str_mv 2013
2013-01-01T00:00:00Z
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/1822/24352
url http://hdl.handle.net/1822/24352
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0927-7765
10.1016/j.colsurfb.2013.01.050
23434718
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 Elsevier
Elsevier BV
publisher.none.fl_str_mv Elsevier
Elsevier BV
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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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
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