Enhancing Antibacterial Activity Against Escherichia coli K-12 of Peptide Ib-AMP4 with Synthetic Analogues

Autores
Flórez Castillo, J. M.; Perullini, Ana Mercedes; Jobbagy, Matias; Cano Calle, Herminsul de Jesús
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A family of Ib-AMP4 peptide analogues was obtained by solid phase synthesis, modifying the net charge and hydrophobicity of C-terminal domain by replacing certain amino acidic residues by arginine and tryptophan. Additionally, disulfide bonds were eliminated by replacing the cysteine residues by methionine, which resulted in a decrease in the number of synthesis byproducts, and consequently diminished the subsequent purification steps. The obtained peptides were purified by RP-HPLC and their molecular mass was determined by MALDI-TOF mass spectrometry. The peptide analogues (IC50 between 1 and 50 μM) presented a higher antibacterial activity against Escherichia coli K-12 than the native peptide (IC50 > 100 μM). The hemolytic activity of the peptide with the highest antibacterial efficacy presented no degradation of erythrocytes for a concentration of 1 μM that corresponds to its IC50 value. The results show that the synthesized peptides are good candidates for the treatment of diseases caused by E. coli.
Fil: Flórez Castillo, J. M.. Universidad Industrial Santander; Colombia
Fil: Perullini, Ana Mercedes. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Jobbagy, Matias. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Cano Calle, Herminsul de Jesús. Universidad Industrial Santander; Colombia
Materia
Péptidos Sintéticos
Pétidos Antifúngicos
Síntesis
Péptidos Biomiméticos
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:11336/30399
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Enhancing Antibacterial Activity Against Escherichia coli K-12 of Peptide Ib-AMP4 with Synthetic AnaloguesFlórez Castillo, J. M.Perullini, Ana MercedesJobbagy, MatiasCano Calle, Herminsul de JesúsPéptidos SintéticosPétidos AntifúngicosSíntesisPéptidos Biomiméticoshttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1A family of Ib-AMP4 peptide analogues was obtained by solid phase synthesis, modifying the net charge and hydrophobicity of C-terminal domain by replacing certain amino acidic residues by arginine and tryptophan. Additionally, disulfide bonds were eliminated by replacing the cysteine residues by methionine, which resulted in a decrease in the number of synthesis byproducts, and consequently diminished the subsequent purification steps. The obtained peptides were purified by RP-HPLC and their molecular mass was determined by MALDI-TOF mass spectrometry. The peptide analogues (IC50 between 1 and 50 μM) presented a higher antibacterial activity against Escherichia coli K-12 than the native peptide (IC50 > 100 μM). The hemolytic activity of the peptide with the highest antibacterial efficacy presented no degradation of erythrocytes for a concentration of 1 μM that corresponds to its IC50 value. The results show that the synthesized peptides are good candidates for the treatment of diseases caused by E. coli.Fil: Flórez Castillo, J. M.. Universidad Industrial Santander; ColombiaFil: Perullini, Ana Mercedes. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; ArgentinaFil: Jobbagy, Matias. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; ArgentinaFil: Cano Calle, Herminsul de Jesús. Universidad Industrial Santander; ColombiaSpringer2014-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/30399Flórez Castillo, J. M.; Perullini, Ana Mercedes; Jobbagy, Matias; Cano Calle, Herminsul de Jesús ; Enhancing Antibacterial Activity Against Escherichia coli K-12 of Peptide Ib-AMP4 with Synthetic Analogues; Springer; International Journal Of Peptide Research And Therapeutics; 20; 3; 1-2014; 365-3691573-31491573-3904CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1007/s10989-014-9391-2info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s10989-014-9391-2info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:00:02Zoai:ri.conicet.gov.ar:11336/30399instacron: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 12:00:03.149CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Enhancing Antibacterial Activity Against Escherichia coli K-12 of Peptide Ib-AMP4 with Synthetic Analogues
title Enhancing Antibacterial Activity Against Escherichia coli K-12 of Peptide Ib-AMP4 with Synthetic Analogues
spellingShingle Enhancing Antibacterial Activity Against Escherichia coli K-12 of Peptide Ib-AMP4 with Synthetic Analogues
Flórez Castillo, J. M.
Péptidos Sintéticos
Pétidos Antifúngicos
Síntesis
Péptidos Biomiméticos
title_short Enhancing Antibacterial Activity Against Escherichia coli K-12 of Peptide Ib-AMP4 with Synthetic Analogues
title_full Enhancing Antibacterial Activity Against Escherichia coli K-12 of Peptide Ib-AMP4 with Synthetic Analogues
title_fullStr Enhancing Antibacterial Activity Against Escherichia coli K-12 of Peptide Ib-AMP4 with Synthetic Analogues
title_full_unstemmed Enhancing Antibacterial Activity Against Escherichia coli K-12 of Peptide Ib-AMP4 with Synthetic Analogues
title_sort Enhancing Antibacterial Activity Against Escherichia coli K-12 of Peptide Ib-AMP4 with Synthetic Analogues
dc.creator.none.fl_str_mv Flórez Castillo, J. M.
Perullini, Ana Mercedes
Jobbagy, Matias
Cano Calle, Herminsul de Jesús
author Flórez Castillo, J. M.
author_facet Flórez Castillo, J. M.
Perullini, Ana Mercedes
Jobbagy, Matias
Cano Calle, Herminsul de Jesús
author_role author
author2 Perullini, Ana Mercedes
Jobbagy, Matias
Cano Calle, Herminsul de Jesús
author2_role author
author
author
dc.subject.none.fl_str_mv Péptidos Sintéticos
Pétidos Antifúngicos
Síntesis
Péptidos Biomiméticos
topic Péptidos Sintéticos
Pétidos Antifúngicos
Síntesis
Péptidos Biomiméticos
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv A family of Ib-AMP4 peptide analogues was obtained by solid phase synthesis, modifying the net charge and hydrophobicity of C-terminal domain by replacing certain amino acidic residues by arginine and tryptophan. Additionally, disulfide bonds were eliminated by replacing the cysteine residues by methionine, which resulted in a decrease in the number of synthesis byproducts, and consequently diminished the subsequent purification steps. The obtained peptides were purified by RP-HPLC and their molecular mass was determined by MALDI-TOF mass spectrometry. The peptide analogues (IC50 between 1 and 50 μM) presented a higher antibacterial activity against Escherichia coli K-12 than the native peptide (IC50 > 100 μM). The hemolytic activity of the peptide with the highest antibacterial efficacy presented no degradation of erythrocytes for a concentration of 1 μM that corresponds to its IC50 value. The results show that the synthesized peptides are good candidates for the treatment of diseases caused by E. coli.
Fil: Flórez Castillo, J. M.. Universidad Industrial Santander; Colombia
Fil: Perullini, Ana Mercedes. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Jobbagy, Matias. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Cano Calle, Herminsul de Jesús. Universidad Industrial Santander; Colombia
description A family of Ib-AMP4 peptide analogues was obtained by solid phase synthesis, modifying the net charge and hydrophobicity of C-terminal domain by replacing certain amino acidic residues by arginine and tryptophan. Additionally, disulfide bonds were eliminated by replacing the cysteine residues by methionine, which resulted in a decrease in the number of synthesis byproducts, and consequently diminished the subsequent purification steps. The obtained peptides were purified by RP-HPLC and their molecular mass was determined by MALDI-TOF mass spectrometry. The peptide analogues (IC50 between 1 and 50 μM) presented a higher antibacterial activity against Escherichia coli K-12 than the native peptide (IC50 > 100 μM). The hemolytic activity of the peptide with the highest antibacterial efficacy presented no degradation of erythrocytes for a concentration of 1 μM that corresponds to its IC50 value. The results show that the synthesized peptides are good candidates for the treatment of diseases caused by E. coli.
publishDate 2014
dc.date.none.fl_str_mv 2014-01
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/11336/30399
Flórez Castillo, J. M.; Perullini, Ana Mercedes; Jobbagy, Matias; Cano Calle, Herminsul de Jesús ; Enhancing Antibacterial Activity Against Escherichia coli K-12 of Peptide Ib-AMP4 with Synthetic Analogues; Springer; International Journal Of Peptide Research And Therapeutics; 20; 3; 1-2014; 365-369
1573-3149
1573-3904
CONICET Digital
CONICET
url http://hdl.handle.net/11336/30399
identifier_str_mv Flórez Castillo, J. M.; Perullini, Ana Mercedes; Jobbagy, Matias; Cano Calle, Herminsul de Jesús ; Enhancing Antibacterial Activity Against Escherichia coli K-12 of Peptide Ib-AMP4 with Synthetic Analogues; Springer; International Journal Of Peptide Research And Therapeutics; 20; 3; 1-2014; 365-369
1573-3149
1573-3904
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1007/s10989-014-9391-2
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s10989-014-9391-2
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 Springer
publisher.none.fl_str_mv Springer
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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