Membrane-peptide interaction: Focusing on membrane properties

Autores
Wilke, Natalia; Alvares, Dayane S.; Crosio, Matias Ariel; Via, Matías Alejandro; Monti, Mariela Roxana; Vargas Velez, Leidy Stefania; Amante, Sofia; Scurti, Pablo; Rulloni, Valeria Soledad
Año de publicación
2023
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Cellular membranes compartmentalize cells, comprise a permeability barrier, and are the starting place for several signaling cascades and processes in which lateral diffusion of molecules is a key factor. Although it has been shown that organisms adapt the lipid composition of their membranes in order to maintain these in a mainly fluid state, several studies point to the coexistence of regions with different compositions and mechanical properties. In this context, while proteins have been related to solid docks, sterols are accepted as liquid-ordered phase state inducers. Thus, the current model for membranes is a patchwork-like surface, with the different regions being highly variable in size and very dynamic. Many peptides, like cationic antimicrobial peptides and cell penetrating peptides, target cell membranes. The affinity of these soluble peptides to membranes depends on membrane features such as composition, charge density, compaction, and fluidity. As a consequence of the patchwork-like character of the membrane, regions with a broad spectrum of properties are available to interact with these peptides. Therefore, it is important to know how peptide-membrane interaction depends on membrane properties, and also what happens with the membranes after the interaction. Here, we summarize our contribution to understanding how the interaction of peptides with membranes is modulated by membrane properties. The influence of the phase state, electrostatics, and chemical composition of the membrane on peptide binding is described using biomimetic systems. The effect of peptide association on membrane properties is also revisited. Finally, possible extrapolations to cells are discussed.
Fil: Wilke, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Alvares, Dayane S.. Universidade Estadual Paulista Julio de Mesquita Filho; Brasil
Fil: Crosio, Matias Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Via, Matías Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Arla Foods a.m.b.a.; Dinamarca
Fil: Monti, Mariela Roxana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Vargas Velez, Leidy Stefania. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Amante, Sofia. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales; Argentina
Fil: Scurti, Pablo. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales; Argentina
Fil: Rulloni, Valeria Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales; Argentina
Materia
Membrane adaptation
Membrane physicochemical properties
Antimicrobial alternative drugs
Membrane-active peptides
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:11336/251676
Acceder
id CONICETDig_7fa1f90b223300f874fe4aa0a9f8d394
oai_identifier_str oai:ri.conicet.gov.ar:11336/251676
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Membrane-peptide interaction: Focusing on membrane propertiesWilke, NataliaAlvares, Dayane S.Crosio, Matias ArielVia, Matías AlejandroMonti, Mariela RoxanaVargas Velez, Leidy StefaniaAmante, SofiaScurti, PabloRulloni, Valeria SoledadMembrane adaptationMembrane physicochemical propertiesAntimicrobial alternative drugsMembrane-active peptideshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Cellular membranes compartmentalize cells, comprise a permeability barrier, and are the starting place for several signaling cascades and processes in which lateral diffusion of molecules is a key factor. Although it has been shown that organisms adapt the lipid composition of their membranes in order to maintain these in a mainly fluid state, several studies point to the coexistence of regions with different compositions and mechanical properties. In this context, while proteins have been related to solid docks, sterols are accepted as liquid-ordered phase state inducers. Thus, the current model for membranes is a patchwork-like surface, with the different regions being highly variable in size and very dynamic. Many peptides, like cationic antimicrobial peptides and cell penetrating peptides, target cell membranes. The affinity of these soluble peptides to membranes depends on membrane features such as composition, charge density, compaction, and fluidity. As a consequence of the patchwork-like character of the membrane, regions with a broad spectrum of properties are available to interact with these peptides. Therefore, it is important to know how peptide-membrane interaction depends on membrane properties, and also what happens with the membranes after the interaction. Here, we summarize our contribution to understanding how the interaction of peptides with membranes is modulated by membrane properties. The influence of the phase state, electrostatics, and chemical composition of the membrane on peptide binding is described using biomimetic systems. The effect of peptide association on membrane properties is also revisited. Finally, possible extrapolations to cells are discussed.Fil: Wilke, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Alvares, Dayane S.. Universidade Estadual Paulista Julio de Mesquita Filho; BrasilFil: Crosio, Matias Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Via, Matías Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Arla Foods a.m.b.a.; DinamarcaFil: Monti, Mariela Roxana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Vargas Velez, Leidy Stefania. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Amante, Sofia. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales; ArgentinaFil: Scurti, Pablo. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales; ArgentinaFil: Rulloni, Valeria Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales; ArgentinaCentro de Estudios sobre Ciencia, Desarrollo y Educación Superior2023-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/251676Wilke, Natalia; Alvares, Dayane S.; Crosio, Matias Ariel; Via, Matías Alejandro; Monti, Mariela Roxana; et al.; Membrane-peptide interaction: Focusing on membrane properties; Centro de Estudios sobre Ciencia, Desarrollo y Educación Superior; Science Reviews - from the end of the world; 2; 3; 10-2023; 21-382683-9288CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.scirevfew.net/index.php/sciencereviews/article/view/46info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:45:40Zoai:ri.conicet.gov.ar:11336/251676instacron: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:34982025-09-29 09:45:40.963CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Membrane-peptide interaction: Focusing on membrane properties
title Membrane-peptide interaction: Focusing on membrane properties
spellingShingle Membrane-peptide interaction: Focusing on membrane properties
Wilke, Natalia
Membrane adaptation
Membrane physicochemical properties
Antimicrobial alternative drugs
Membrane-active peptides
title_short Membrane-peptide interaction: Focusing on membrane properties
title_full Membrane-peptide interaction: Focusing on membrane properties
title_fullStr Membrane-peptide interaction: Focusing on membrane properties
title_full_unstemmed Membrane-peptide interaction: Focusing on membrane properties
title_sort Membrane-peptide interaction: Focusing on membrane properties
dc.creator.none.fl_str_mv Wilke, Natalia
Alvares, Dayane S.
Crosio, Matias Ariel
Via, Matías Alejandro
Monti, Mariela Roxana
Vargas Velez, Leidy Stefania
Amante, Sofia
Scurti, Pablo
Rulloni, Valeria Soledad
author Wilke, Natalia
author_facet Wilke, Natalia
Alvares, Dayane S.
Crosio, Matias Ariel
Via, Matías Alejandro
Monti, Mariela Roxana
Vargas Velez, Leidy Stefania
Amante, Sofia
Scurti, Pablo
Rulloni, Valeria Soledad
author_role author
author2 Alvares, Dayane S.
Crosio, Matias Ariel
Via, Matías Alejandro
Monti, Mariela Roxana
Vargas Velez, Leidy Stefania
Amante, Sofia
Scurti, Pablo
Rulloni, Valeria Soledad
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Membrane adaptation
Membrane physicochemical properties
Antimicrobial alternative drugs
Membrane-active peptides
topic Membrane adaptation
Membrane physicochemical properties
Antimicrobial alternative drugs
Membrane-active peptides
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Cellular membranes compartmentalize cells, comprise a permeability barrier, and are the starting place for several signaling cascades and processes in which lateral diffusion of molecules is a key factor. Although it has been shown that organisms adapt the lipid composition of their membranes in order to maintain these in a mainly fluid state, several studies point to the coexistence of regions with different compositions and mechanical properties. In this context, while proteins have been related to solid docks, sterols are accepted as liquid-ordered phase state inducers. Thus, the current model for membranes is a patchwork-like surface, with the different regions being highly variable in size and very dynamic. Many peptides, like cationic antimicrobial peptides and cell penetrating peptides, target cell membranes. The affinity of these soluble peptides to membranes depends on membrane features such as composition, charge density, compaction, and fluidity. As a consequence of the patchwork-like character of the membrane, regions with a broad spectrum of properties are available to interact with these peptides. Therefore, it is important to know how peptide-membrane interaction depends on membrane properties, and also what happens with the membranes after the interaction. Here, we summarize our contribution to understanding how the interaction of peptides with membranes is modulated by membrane properties. The influence of the phase state, electrostatics, and chemical composition of the membrane on peptide binding is described using biomimetic systems. The effect of peptide association on membrane properties is also revisited. Finally, possible extrapolations to cells are discussed.
Fil: Wilke, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Alvares, Dayane S.. Universidade Estadual Paulista Julio de Mesquita Filho; Brasil
Fil: Crosio, Matias Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Via, Matías Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Arla Foods a.m.b.a.; Dinamarca
Fil: Monti, Mariela Roxana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Vargas Velez, Leidy Stefania. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Amante, Sofia. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales; Argentina
Fil: Scurti, Pablo. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales; Argentina
Fil: Rulloni, Valeria Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales; Argentina
description Cellular membranes compartmentalize cells, comprise a permeability barrier, and are the starting place for several signaling cascades and processes in which lateral diffusion of molecules is a key factor. Although it has been shown that organisms adapt the lipid composition of their membranes in order to maintain these in a mainly fluid state, several studies point to the coexistence of regions with different compositions and mechanical properties. In this context, while proteins have been related to solid docks, sterols are accepted as liquid-ordered phase state inducers. Thus, the current model for membranes is a patchwork-like surface, with the different regions being highly variable in size and very dynamic. Many peptides, like cationic antimicrobial peptides and cell penetrating peptides, target cell membranes. The affinity of these soluble peptides to membranes depends on membrane features such as composition, charge density, compaction, and fluidity. As a consequence of the patchwork-like character of the membrane, regions with a broad spectrum of properties are available to interact with these peptides. Therefore, it is important to know how peptide-membrane interaction depends on membrane properties, and also what happens with the membranes after the interaction. Here, we summarize our contribution to understanding how the interaction of peptides with membranes is modulated by membrane properties. The influence of the phase state, electrostatics, and chemical composition of the membrane on peptide binding is described using biomimetic systems. The effect of peptide association on membrane properties is also revisited. Finally, possible extrapolations to cells are discussed.
publishDate 2023
dc.date.none.fl_str_mv 2023-10
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/11336/251676
Wilke, Natalia; Alvares, Dayane S.; Crosio, Matias Ariel; Via, Matías Alejandro; Monti, Mariela Roxana; et al.; Membrane-peptide interaction: Focusing on membrane properties; Centro de Estudios sobre Ciencia, Desarrollo y Educación Superior; Science Reviews - from the end of the world; 2; 3; 10-2023; 21-38
2683-9288
CONICET Digital
CONICET
url http://hdl.handle.net/11336/251676
identifier_str_mv Wilke, Natalia; Alvares, Dayane S.; Crosio, Matias Ariel; Via, Matías Alejandro; Monti, Mariela Roxana; et al.; Membrane-peptide interaction: Focusing on membrane properties; Centro de Estudios sobre Ciencia, Desarrollo y Educación Superior; Science Reviews - from the end of the world; 2; 3; 10-2023; 21-38
2683-9288
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.scirevfew.net/index.php/sciencereviews/article/view/46
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
dc.publisher.none.fl_str_mv Centro de Estudios sobre Ciencia, Desarrollo y Educación Superior
publisher.none.fl_str_mv Centro de Estudios sobre Ciencia, Desarrollo y Educación Superior
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 13.070432

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