Filling gaps in the knowledge of melittin on lipid membranes

Autores
Elias Tissera, Maria Jose; Disalvo, Edgardo Anibal; Martini, María Florencia; Cutró, Andrea Carmen
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Melittin (ML) is a small peptide of 26 residues rich in arginine (Arg) and lysine (Lys). Several studies have been done to understand the mechanism of interaction with neutral and negatively charged lipids. However, it is not known with certainty how this interaction depends on the electrostatic or hydrophobic forces according to the composition of the membrane, nor with the different organization of lipids on the membrane, such as the microdomains that could take place in it. Therefore, comparative studies of the interaction and the effect of ML with respect to cationic peptides (Arg-7 and Lys-5) were conducted to get a deeper insight of the ML interaction mechanism with membranes. In this regard, measurements of zeta potential of different model membranes (DOPC, DMPC and DMPE liposomes) in the presence of the peptides, and molecular dynamics simulations were performed. In the special case of DMPC, we worked in its gel like-ripple phase, in order to analyzed defects of packing that potentially expose hydrocarbon regions. In relation with experimental results, molecular analysis of ML interaction with zwiterionic lipid membrane in its ripple phase was performed by unbiased molecular dynamics simulations. The results allow us to remark that ML penetration is favored in the gel-liquid crystalline phase transition in zwitterionic lipids. The importance of this study lies in the understanding of the first stages of action of the ML in eukaryotic membranes, in model systems of its main lipid composition.
Fil: Elias Tissera, Maria Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Disalvo, Edgardo Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Martini, María Florencia. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Farmacología. Cátedra de Química Medicinal; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Metabolismo del Fármaco. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Metabolismo del Fármaco; Argentina
Fil: Cutró, Andrea Carmen. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Materia
LIPID COMPOSITION
LIPID ORGANIZATION
MELITTIN
MELITTIN-LIPID MEMBRANE INTERACTION
MOLECULAR DYNAMIC SIMULATIONS
ZETA POTENTIAL
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/86999
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/86999
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Filling gaps in the knowledge of melittin on lipid membranesElias Tissera, Maria JoseDisalvo, Edgardo AnibalMartini, María FlorenciaCutró, Andrea CarmenLIPID COMPOSITIONLIPID ORGANIZATIONMELITTINMELITTIN-LIPID MEMBRANE INTERACTIONMOLECULAR DYNAMIC SIMULATIONSZETA POTENTIALhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Melittin (ML) is a small peptide of 26 residues rich in arginine (Arg) and lysine (Lys). Several studies have been done to understand the mechanism of interaction with neutral and negatively charged lipids. However, it is not known with certainty how this interaction depends on the electrostatic or hydrophobic forces according to the composition of the membrane, nor with the different organization of lipids on the membrane, such as the microdomains that could take place in it. Therefore, comparative studies of the interaction and the effect of ML with respect to cationic peptides (Arg-7 and Lys-5) were conducted to get a deeper insight of the ML interaction mechanism with membranes. In this regard, measurements of zeta potential of different model membranes (DOPC, DMPC and DMPE liposomes) in the presence of the peptides, and molecular dynamics simulations were performed. In the special case of DMPC, we worked in its gel like-ripple phase, in order to analyzed defects of packing that potentially expose hydrocarbon regions. In relation with experimental results, molecular analysis of ML interaction with zwiterionic lipid membrane in its ripple phase was performed by unbiased molecular dynamics simulations. The results allow us to remark that ML penetration is favored in the gel-liquid crystalline phase transition in zwitterionic lipids. The importance of this study lies in the understanding of the first stages of action of the ML in eukaryotic membranes, in model systems of its main lipid composition.Fil: Elias Tissera, Maria Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; ArgentinaFil: Disalvo, Edgardo Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; ArgentinaFil: Martini, María Florencia. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Farmacología. Cátedra de Química Medicinal; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Metabolismo del Fármaco. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Metabolismo del Fármaco; ArgentinaFil: Cutró, Andrea Carmen. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; ArgentinaElsevier Science2019-01-21info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/86999Elias Tissera, Maria Jose; Disalvo, Edgardo Anibal; Martini, María Florencia; Cutró, Andrea Carmen; Filling gaps in the knowledge of melittin on lipid membranes; Elsevier Science; Colloids and Surfaces A: Physicochemical and Engineering Aspects; 561; 21-1-2019; 136-1460927-7757CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.colsurfa.2018.10.055info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0927775718309208info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:06:35Zoai:ri.conicet.gov.ar:11336/86999instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 12:06:36.252CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Filling gaps in the knowledge of melittin on lipid membranes
title Filling gaps in the knowledge of melittin on lipid membranes
spellingShingle Filling gaps in the knowledge of melittin on lipid membranes
Elias Tissera, Maria Jose
LIPID COMPOSITION
LIPID ORGANIZATION
MELITTIN
MELITTIN-LIPID MEMBRANE INTERACTION
MOLECULAR DYNAMIC SIMULATIONS
ZETA POTENTIAL
title_short Filling gaps in the knowledge of melittin on lipid membranes
title_full Filling gaps in the knowledge of melittin on lipid membranes
title_fullStr Filling gaps in the knowledge of melittin on lipid membranes
title_full_unstemmed Filling gaps in the knowledge of melittin on lipid membranes
title_sort Filling gaps in the knowledge of melittin on lipid membranes
dc.creator.none.fl_str_mv Elias Tissera, Maria Jose
Disalvo, Edgardo Anibal
Martini, María Florencia
Cutró, Andrea Carmen
author Elias Tissera, Maria Jose
author_facet Elias Tissera, Maria Jose
Disalvo, Edgardo Anibal
Martini, María Florencia
Cutró, Andrea Carmen
author_role author
author2 Disalvo, Edgardo Anibal
Martini, María Florencia
Cutró, Andrea Carmen
author2_role author
author
author
dc.subject.none.fl_str_mv LIPID COMPOSITION
LIPID ORGANIZATION
MELITTIN
MELITTIN-LIPID MEMBRANE INTERACTION
MOLECULAR DYNAMIC SIMULATIONS
ZETA POTENTIAL
topic LIPID COMPOSITION
LIPID ORGANIZATION
MELITTIN
MELITTIN-LIPID MEMBRANE INTERACTION
MOLECULAR DYNAMIC SIMULATIONS
ZETA POTENTIAL
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Melittin (ML) is a small peptide of 26 residues rich in arginine (Arg) and lysine (Lys). Several studies have been done to understand the mechanism of interaction with neutral and negatively charged lipids. However, it is not known with certainty how this interaction depends on the electrostatic or hydrophobic forces according to the composition of the membrane, nor with the different organization of lipids on the membrane, such as the microdomains that could take place in it. Therefore, comparative studies of the interaction and the effect of ML with respect to cationic peptides (Arg-7 and Lys-5) were conducted to get a deeper insight of the ML interaction mechanism with membranes. In this regard, measurements of zeta potential of different model membranes (DOPC, DMPC and DMPE liposomes) in the presence of the peptides, and molecular dynamics simulations were performed. In the special case of DMPC, we worked in its gel like-ripple phase, in order to analyzed defects of packing that potentially expose hydrocarbon regions. In relation with experimental results, molecular analysis of ML interaction with zwiterionic lipid membrane in its ripple phase was performed by unbiased molecular dynamics simulations. The results allow us to remark that ML penetration is favored in the gel-liquid crystalline phase transition in zwitterionic lipids. The importance of this study lies in the understanding of the first stages of action of the ML in eukaryotic membranes, in model systems of its main lipid composition.
Fil: Elias Tissera, Maria Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Disalvo, Edgardo Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Martini, María Florencia. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Farmacología. Cátedra de Química Medicinal; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Metabolismo del Fármaco. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Metabolismo del Fármaco; Argentina
Fil: Cutró, Andrea Carmen. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
description Melittin (ML) is a small peptide of 26 residues rich in arginine (Arg) and lysine (Lys). Several studies have been done to understand the mechanism of interaction with neutral and negatively charged lipids. However, it is not known with certainty how this interaction depends on the electrostatic or hydrophobic forces according to the composition of the membrane, nor with the different organization of lipids on the membrane, such as the microdomains that could take place in it. Therefore, comparative studies of the interaction and the effect of ML with respect to cationic peptides (Arg-7 and Lys-5) were conducted to get a deeper insight of the ML interaction mechanism with membranes. In this regard, measurements of zeta potential of different model membranes (DOPC, DMPC and DMPE liposomes) in the presence of the peptides, and molecular dynamics simulations were performed. In the special case of DMPC, we worked in its gel like-ripple phase, in order to analyzed defects of packing that potentially expose hydrocarbon regions. In relation with experimental results, molecular analysis of ML interaction with zwiterionic lipid membrane in its ripple phase was performed by unbiased molecular dynamics simulations. The results allow us to remark that ML penetration is favored in the gel-liquid crystalline phase transition in zwitterionic lipids. The importance of this study lies in the understanding of the first stages of action of the ML in eukaryotic membranes, in model systems of its main lipid composition.
publishDate 2019
dc.date.none.fl_str_mv 2019-01-21
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/86999
Elias Tissera, Maria Jose; Disalvo, Edgardo Anibal; Martini, María Florencia; Cutró, Andrea Carmen; Filling gaps in the knowledge of melittin on lipid membranes; Elsevier Science; Colloids and Surfaces A: Physicochemical and Engineering Aspects; 561; 21-1-2019; 136-146
0927-7757
CONICET Digital
CONICET
url http://hdl.handle.net/11336/86999
identifier_str_mv Elias Tissera, Maria Jose; Disalvo, Edgardo Anibal; Martini, María Florencia; Cutró, Andrea Carmen; Filling gaps in the knowledge of melittin on lipid membranes; Elsevier Science; Colloids and Surfaces A: Physicochemical and Engineering Aspects; 561; 21-1-2019; 136-146
0927-7757
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.colsurfa.2018.10.055
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0927775718309208
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.982451

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