28-mer fragment derived from Enterocin CRL35 displays an unexpected bactericidal effect on listeria cells

Autores
Masias, Ruth Emilse; da Silva Sanches, Paulo Ricardo; Dupuy, Fernando Gabriel; Acuña, Leonardo; Bellomio, Augusto; Cilli, Eduardo; Saavedra, Maria Lucila; Minahk, Carlos Javier
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Two shorter peptides derived from enterocin CRL35, a 43-mer bacteriocin, were synthesized i.e. the N-terminal fragment spanning from residues 1 to 15, and a 28-mer fragment that represents the C-terminal of enterocin CRL35, the residues 16 to 43. The separate peptides showed no activity when combined. On one hand, the 28-mer peptide displayed an unpredicted antimicrobial activity. On the other, 15- mer peptide had no consistent anti-Listeria effect. The dissociation constants calculated from experimental data indicated that all peptides could bind at similar extent to the sensitive cells. However, transmembrane electrical potential was not dissipated to the same level by the different peptides; whereas the full-length and the C-terminal 28-mer fragment induced almost full dissipation, 15-mer fragment produced only a slow and incomplete effect. Furthermore, a different interaction of each peptide with membranes was demonstrated based on studies carried out with liposomes, which led us to conclude that activity was related to structure rather than to net positive charges. These results open up the possibility of designing new peptides based on the 28-mer fragment with enhanced activity, which would represent a promising approach for combating Listeria and other pathogens.
Fil: Masias, Ruth Emilse. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: da Silva Sanches, Paulo Ricardo. Universidade Estadual Paulista Julio de Mesquita Filho; Brasil
Fil: Dupuy, Fernando Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Acuña, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Bellomio, Augusto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Cilli, Eduardo. Universidade Estadual Paulista Julio de Mesquita Filho; Brasil
Fil: Saavedra, Maria Lucila. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Minahk, Carlos Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Materia
Bacteriocins
Enterocin Crl35
Listeria
Synthetic 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:11336/28427
Acceder
id CONICETDig_7f60bdcb548d3a91f0875d57ca164f99
oai_identifier_str oai:ri.conicet.gov.ar:11336/28427
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 28-mer fragment derived from Enterocin CRL35 displays an unexpected bactericidal effect on listeria cellsMasias, Ruth Emilseda Silva Sanches, Paulo RicardoDupuy, Fernando GabrielAcuña, LeonardoBellomio, AugustoCilli, EduardoSaavedra, Maria LucilaMinahk, Carlos JavierBacteriocinsEnterocin Crl35ListeriaSynthetic Peptideshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Two shorter peptides derived from enterocin CRL35, a 43-mer bacteriocin, were synthesized i.e. the N-terminal fragment spanning from residues 1 to 15, and a 28-mer fragment that represents the C-terminal of enterocin CRL35, the residues 16 to 43. The separate peptides showed no activity when combined. On one hand, the 28-mer peptide displayed an unpredicted antimicrobial activity. On the other, 15- mer peptide had no consistent anti-Listeria effect. The dissociation constants calculated from experimental data indicated that all peptides could bind at similar extent to the sensitive cells. However, transmembrane electrical potential was not dissipated to the same level by the different peptides; whereas the full-length and the C-terminal 28-mer fragment induced almost full dissipation, 15-mer fragment produced only a slow and incomplete effect. Furthermore, a different interaction of each peptide with membranes was demonstrated based on studies carried out with liposomes, which led us to conclude that activity was related to structure rather than to net positive charges. These results open up the possibility of designing new peptides based on the 28-mer fragment with enhanced activity, which would represent a promising approach for combating Listeria and other pathogens.Fil: Masias, Ruth Emilse. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: da Silva Sanches, Paulo Ricardo. Universidade Estadual Paulista Julio de Mesquita Filho; BrasilFil: Dupuy, Fernando Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Acuña, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Bellomio, Augusto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Cilli, Eduardo. Universidade Estadual Paulista Julio de Mesquita Filho; BrasilFil: Saavedra, Maria Lucila. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: Minahk, Carlos Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaBentham Science Publishers2015-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/28427Masias, Ruth Emilse; da Silva Sanches, Paulo Ricardo; Dupuy, Fernando Gabriel; Acuña, Leonardo; Bellomio, Augusto; et al.; 28-mer fragment derived from Enterocin CRL35 displays an unexpected bactericidal effect on listeria cells; Bentham Science Publishers; Protein and Peptide Letters; 22; 6; 5-2015; 482-4880929-86651875-5305CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.2174/0929866522666150506094300info:eu-repo/semantics/altIdentifier/url/http://www.eurekaselect.com/131041/articleinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:17:36Zoai:ri.conicet.gov.ar:11336/28427instacron: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 10:17:36.676CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv 28-mer fragment derived from Enterocin CRL35 displays an unexpected bactericidal effect on listeria cells
title 28-mer fragment derived from Enterocin CRL35 displays an unexpected bactericidal effect on listeria cells
spellingShingle 28-mer fragment derived from Enterocin CRL35 displays an unexpected bactericidal effect on listeria cells
Masias, Ruth Emilse
Bacteriocins
Enterocin Crl35
Listeria
Synthetic Peptides
title_short 28-mer fragment derived from Enterocin CRL35 displays an unexpected bactericidal effect on listeria cells
title_full 28-mer fragment derived from Enterocin CRL35 displays an unexpected bactericidal effect on listeria cells
title_fullStr 28-mer fragment derived from Enterocin CRL35 displays an unexpected bactericidal effect on listeria cells
title_full_unstemmed 28-mer fragment derived from Enterocin CRL35 displays an unexpected bactericidal effect on listeria cells
title_sort 28-mer fragment derived from Enterocin CRL35 displays an unexpected bactericidal effect on listeria cells
dc.creator.none.fl_str_mv Masias, Ruth Emilse
da Silva Sanches, Paulo Ricardo
Dupuy, Fernando Gabriel
Acuña, Leonardo
Bellomio, Augusto
Cilli, Eduardo
Saavedra, Maria Lucila
Minahk, Carlos Javier
author Masias, Ruth Emilse
author_facet Masias, Ruth Emilse
da Silva Sanches, Paulo Ricardo
Dupuy, Fernando Gabriel
Acuña, Leonardo
Bellomio, Augusto
Cilli, Eduardo
Saavedra, Maria Lucila
Minahk, Carlos Javier
author_role author
author2 da Silva Sanches, Paulo Ricardo
Dupuy, Fernando Gabriel
Acuña, Leonardo
Bellomio, Augusto
Cilli, Eduardo
Saavedra, Maria Lucila
Minahk, Carlos Javier
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Bacteriocins
Enterocin Crl35
Listeria
Synthetic Peptides
topic Bacteriocins
Enterocin Crl35
Listeria
Synthetic 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 Two shorter peptides derived from enterocin CRL35, a 43-mer bacteriocin, were synthesized i.e. the N-terminal fragment spanning from residues 1 to 15, and a 28-mer fragment that represents the C-terminal of enterocin CRL35, the residues 16 to 43. The separate peptides showed no activity when combined. On one hand, the 28-mer peptide displayed an unpredicted antimicrobial activity. On the other, 15- mer peptide had no consistent anti-Listeria effect. The dissociation constants calculated from experimental data indicated that all peptides could bind at similar extent to the sensitive cells. However, transmembrane electrical potential was not dissipated to the same level by the different peptides; whereas the full-length and the C-terminal 28-mer fragment induced almost full dissipation, 15-mer fragment produced only a slow and incomplete effect. Furthermore, a different interaction of each peptide with membranes was demonstrated based on studies carried out with liposomes, which led us to conclude that activity was related to structure rather than to net positive charges. These results open up the possibility of designing new peptides based on the 28-mer fragment with enhanced activity, which would represent a promising approach for combating Listeria and other pathogens.
Fil: Masias, Ruth Emilse. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: da Silva Sanches, Paulo Ricardo. Universidade Estadual Paulista Julio de Mesquita Filho; Brasil
Fil: Dupuy, Fernando Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Acuña, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Bellomio, Augusto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Cilli, Eduardo. Universidade Estadual Paulista Julio de Mesquita Filho; Brasil
Fil: Saavedra, Maria Lucila. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Minahk, Carlos Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
description Two shorter peptides derived from enterocin CRL35, a 43-mer bacteriocin, were synthesized i.e. the N-terminal fragment spanning from residues 1 to 15, and a 28-mer fragment that represents the C-terminal of enterocin CRL35, the residues 16 to 43. The separate peptides showed no activity when combined. On one hand, the 28-mer peptide displayed an unpredicted antimicrobial activity. On the other, 15- mer peptide had no consistent anti-Listeria effect. The dissociation constants calculated from experimental data indicated that all peptides could bind at similar extent to the sensitive cells. However, transmembrane electrical potential was not dissipated to the same level by the different peptides; whereas the full-length and the C-terminal 28-mer fragment induced almost full dissipation, 15-mer fragment produced only a slow and incomplete effect. Furthermore, a different interaction of each peptide with membranes was demonstrated based on studies carried out with liposomes, which led us to conclude that activity was related to structure rather than to net positive charges. These results open up the possibility of designing new peptides based on the 28-mer fragment with enhanced activity, which would represent a promising approach for combating Listeria and other pathogens.
publishDate 2015
dc.date.none.fl_str_mv 2015-05
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/11336/28427
Masias, Ruth Emilse; da Silva Sanches, Paulo Ricardo; Dupuy, Fernando Gabriel; Acuña, Leonardo; Bellomio, Augusto; et al.; 28-mer fragment derived from Enterocin CRL35 displays an unexpected bactericidal effect on listeria cells; Bentham Science Publishers; Protein and Peptide Letters; 22; 6; 5-2015; 482-488
0929-8665
1875-5305
CONICET Digital
CONICET
url http://hdl.handle.net/11336/28427
identifier_str_mv Masias, Ruth Emilse; da Silva Sanches, Paulo Ricardo; Dupuy, Fernando Gabriel; Acuña, Leonardo; Bellomio, Augusto; et al.; 28-mer fragment derived from Enterocin CRL35 displays an unexpected bactericidal effect on listeria cells; Bentham Science Publishers; Protein and Peptide Letters; 22; 6; 5-2015; 482-488
0929-8665
1875-5305
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.2174/0929866522666150506094300
info:eu-repo/semantics/altIdentifier/url/http://www.eurekaselect.com/131041/article
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
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Bentham Science Publishers
publisher.none.fl_str_mv Bentham Science Publishers
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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