Adsorption of pH-sensitive peptides on self-assembled lipid membranes

Autores
Chiarpotti, María V.; del Popolo, Mario Gabriel; Longo, Gabriel Sebastian
Año de publicación
2022
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Experiments have shown that the pH is low in the vicinity of tumor cells. The acidity contrast between diseased and healthy tissues offers the possibility of developing pH-sensitive chemical markers that allow the identification and treatment of tumors. In particular, peptides possessing pH-Sensitive amino acids can be used as vehicles to introduce therapeutic and contrast agents into cancer cells. In this work, we present a model based on Molecular Theory [1] that allows us to study the adsorption and insertion of pH-sensitive peptides in lipid membranes. In particular, we focus on a set of cyclic peptides developed by Weerakkody et al. that is effective in the identification and treatment of tumors [2]. Peptides and lipids are described by a coarse-grained model based on the MARTINI force field. A free energy functional is proposed whose minimization leads to the self-aggregation of lipid molecules to form a membrane, and to the spatial distribution of peptides and ions through the lipid/solution interface. Our methodology considers electrostatic and steric interactions, entropic effects, and the acid-base equilibrium of all titratable molecules. In addition, the theory considers the shape, charge distribution, and conformations of lipids and peptides. First, we characterize the membrane self-assembly. Second, we characterize the adsorption and insertion of two cyclic peptides, c[E4W5C] and c[R4W5C], and a linear peptide, l[CW(EW)4], as a function of the pH of the solution. Two lipid membranes are considered, a neutral and a titratable one. The results are presented at pH 3 and 8 ensuring the complete charge transition of glutamate residues. Our results allow us to test the adsorption mechanism of the peptides, which are compared with experimental data [2].
Fil: Chiarpotti, María V.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto Interdisciplinario de Ciencias Básicas. - Universidad Nacional de Cuyo. Instituto Interdisciplinario de Ciencias Básicas; Argentina
Fil: del Popolo, Mario Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto Interdisciplinario de Ciencias Básicas. - Universidad Nacional de Cuyo. Instituto Interdisciplinario de Ciencias Básicas; Argentina
Fil: Longo, Gabriel Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina
L Reunión Anual de la Sociedad Argentina de Biofísica
Rosario
Argentina
Sociedad Argentina de Biofísica
Materia
PH-SENSITIVE PEPTIDES
LIPID MEMBRANES
TUMOR MICROENVIRONMENT
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:11336/275631
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/275631
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Adsorption of pH-sensitive peptides on self-assembled lipid membranesChiarpotti, María V.del Popolo, Mario GabrielLongo, Gabriel SebastianPH-SENSITIVE PEPTIDESLIPID MEMBRANESTUMOR MICROENVIRONMENThttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Experiments have shown that the pH is low in the vicinity of tumor cells. The acidity contrast between diseased and healthy tissues offers the possibility of developing pH-sensitive chemical markers that allow the identification and treatment of tumors. In particular, peptides possessing pH-Sensitive amino acids can be used as vehicles to introduce therapeutic and contrast agents into cancer cells. In this work, we present a model based on Molecular Theory [1] that allows us to study the adsorption and insertion of pH-sensitive peptides in lipid membranes. In particular, we focus on a set of cyclic peptides developed by Weerakkody et al. that is effective in the identification and treatment of tumors [2]. Peptides and lipids are described by a coarse-grained model based on the MARTINI force field. A free energy functional is proposed whose minimization leads to the self-aggregation of lipid molecules to form a membrane, and to the spatial distribution of peptides and ions through the lipid/solution interface. Our methodology considers electrostatic and steric interactions, entropic effects, and the acid-base equilibrium of all titratable molecules. In addition, the theory considers the shape, charge distribution, and conformations of lipids and peptides. First, we characterize the membrane self-assembly. Second, we characterize the adsorption and insertion of two cyclic peptides, c[E4W5C] and c[R4W5C], and a linear peptide, l[CW(EW)4], as a function of the pH of the solution. Two lipid membranes are considered, a neutral and a titratable one. The results are presented at pH 3 and 8 ensuring the complete charge transition of glutamate residues. Our results allow us to test the adsorption mechanism of the peptides, which are compared with experimental data [2].Fil: Chiarpotti, María V.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto Interdisciplinario de Ciencias Básicas. - Universidad Nacional de Cuyo. Instituto Interdisciplinario de Ciencias Básicas; ArgentinaFil: del Popolo, Mario Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto Interdisciplinario de Ciencias Básicas. - Universidad Nacional de Cuyo. Instituto Interdisciplinario de Ciencias Básicas; ArgentinaFil: Longo, Gabriel Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; ArgentinaL Reunión Anual de la Sociedad Argentina de BiofísicaRosarioArgentinaSociedad Argentina de BiofísicaSociedad Argentina de Biofísica2022info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/275631Adsorption of pH-sensitive peptides on self-assembled lipid membranes; L Reunión Anual de la Sociedad Argentina de Biofísica; Rosario; Argentina; 2022; 102-102978-987-48938-0-2CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/publicaciones/libros-de-resumenes/Internacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-12-23T13:19:59Zoai:ri.conicet.gov.ar:11336/275631instacron: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:34982025-12-23 13:19:59.376CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Adsorption of pH-sensitive peptides on self-assembled lipid membranes
title Adsorption of pH-sensitive peptides on self-assembled lipid membranes
spellingShingle Adsorption of pH-sensitive peptides on self-assembled lipid membranes
Chiarpotti, María V.
PH-SENSITIVE PEPTIDES
LIPID MEMBRANES
TUMOR MICROENVIRONMENT
title_short Adsorption of pH-sensitive peptides on self-assembled lipid membranes
title_full Adsorption of pH-sensitive peptides on self-assembled lipid membranes
title_fullStr Adsorption of pH-sensitive peptides on self-assembled lipid membranes
title_full_unstemmed Adsorption of pH-sensitive peptides on self-assembled lipid membranes
title_sort Adsorption of pH-sensitive peptides on self-assembled lipid membranes
dc.creator.none.fl_str_mv Chiarpotti, María V.
del Popolo, Mario Gabriel
Longo, Gabriel Sebastian
author Chiarpotti, María V.
author_facet Chiarpotti, María V.
del Popolo, Mario Gabriel
Longo, Gabriel Sebastian
author_role author
author2 del Popolo, Mario Gabriel
Longo, Gabriel Sebastian
author2_role author
author
dc.subject.none.fl_str_mv PH-SENSITIVE PEPTIDES
LIPID MEMBRANES
TUMOR MICROENVIRONMENT
topic PH-SENSITIVE PEPTIDES
LIPID MEMBRANES
TUMOR MICROENVIRONMENT
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Experiments have shown that the pH is low in the vicinity of tumor cells. The acidity contrast between diseased and healthy tissues offers the possibility of developing pH-sensitive chemical markers that allow the identification and treatment of tumors. In particular, peptides possessing pH-Sensitive amino acids can be used as vehicles to introduce therapeutic and contrast agents into cancer cells. In this work, we present a model based on Molecular Theory [1] that allows us to study the adsorption and insertion of pH-sensitive peptides in lipid membranes. In particular, we focus on a set of cyclic peptides developed by Weerakkody et al. that is effective in the identification and treatment of tumors [2]. Peptides and lipids are described by a coarse-grained model based on the MARTINI force field. A free energy functional is proposed whose minimization leads to the self-aggregation of lipid molecules to form a membrane, and to the spatial distribution of peptides and ions through the lipid/solution interface. Our methodology considers electrostatic and steric interactions, entropic effects, and the acid-base equilibrium of all titratable molecules. In addition, the theory considers the shape, charge distribution, and conformations of lipids and peptides. First, we characterize the membrane self-assembly. Second, we characterize the adsorption and insertion of two cyclic peptides, c[E4W5C] and c[R4W5C], and a linear peptide, l[CW(EW)4], as a function of the pH of the solution. Two lipid membranes are considered, a neutral and a titratable one. The results are presented at pH 3 and 8 ensuring the complete charge transition of glutamate residues. Our results allow us to test the adsorption mechanism of the peptides, which are compared with experimental data [2].
Fil: Chiarpotti, María V.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto Interdisciplinario de Ciencias Básicas. - Universidad Nacional de Cuyo. Instituto Interdisciplinario de Ciencias Básicas; Argentina
Fil: del Popolo, Mario Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto Interdisciplinario de Ciencias Básicas. - Universidad Nacional de Cuyo. Instituto Interdisciplinario de Ciencias Básicas; Argentina
Fil: Longo, Gabriel Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina
L Reunión Anual de la Sociedad Argentina de Biofísica
Rosario
Argentina
Sociedad Argentina de Biofísica
description Experiments have shown that the pH is low in the vicinity of tumor cells. The acidity contrast between diseased and healthy tissues offers the possibility of developing pH-sensitive chemical markers that allow the identification and treatment of tumors. In particular, peptides possessing pH-Sensitive amino acids can be used as vehicles to introduce therapeutic and contrast agents into cancer cells. In this work, we present a model based on Molecular Theory [1] that allows us to study the adsorption and insertion of pH-sensitive peptides in lipid membranes. In particular, we focus on a set of cyclic peptides developed by Weerakkody et al. that is effective in the identification and treatment of tumors [2]. Peptides and lipids are described by a coarse-grained model based on the MARTINI force field. A free energy functional is proposed whose minimization leads to the self-aggregation of lipid molecules to form a membrane, and to the spatial distribution of peptides and ions through the lipid/solution interface. Our methodology considers electrostatic and steric interactions, entropic effects, and the acid-base equilibrium of all titratable molecules. In addition, the theory considers the shape, charge distribution, and conformations of lipids and peptides. First, we characterize the membrane self-assembly. Second, we characterize the adsorption and insertion of two cyclic peptides, c[E4W5C] and c[R4W5C], and a linear peptide, l[CW(EW)4], as a function of the pH of the solution. Two lipid membranes are considered, a neutral and a titratable one. The results are presented at pH 3 and 8 ensuring the complete charge transition of glutamate residues. Our results allow us to test the adsorption mechanism of the peptides, which are compared with experimental data [2].
publishDate 2022
dc.date.none.fl_str_mv 2022
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Reunión
Book
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/275631
Adsorption of pH-sensitive peptides on self-assembled lipid membranes; L Reunión Anual de la Sociedad Argentina de Biofísica; Rosario; Argentina; 2022; 102-102
978-987-48938-0-2
CONICET Digital
CONICET
url http://hdl.handle.net/11336/275631
identifier_str_mv Adsorption of pH-sensitive peptides on self-assembled lipid membranes; L Reunión Anual de la Sociedad Argentina de Biofísica; Rosario; Argentina; 2022; 102-102
978-987-48938-0-2
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://biofisica.org.ar/publicaciones/libros-de-resumenes/
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.coverage.none.fl_str_mv Internacional
dc.publisher.none.fl_str_mv Sociedad Argentina de Biofísica
publisher.none.fl_str_mv Sociedad Argentina de Biofísica
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
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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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