The activity of LE10 peptide on biological membranes using molecular dynamics, in vitro and in vivo studies
Autor(a) principal: | |
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Data de Publicação: | 2013 |
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/1822/24352 |
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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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 |
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 |
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1799132219905671168 |