Interaction of acylated and substituted antimicrobial peptide analogs with phospholipid-polydiacetylene vesicles. Correlation with their biological properties

Autores
Siano, Alvaro Sebastían; Húmpola, Maria Veronica; Rey, María Carolina; Simonetta, Arturo Carlos; Tonarelli, Georgina Guadalupe
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A series of peptide analogs based on region 6-22 of Plantaricin 149 sequence were synthesized. The interaction between these analogs and phospholipid-polydiacetylene vesicles was investigated to evaluate the ability of the bioassay to detect differences in the interaction of the peptides with dipalmitoylphosphatidylglycerol and dipalmitoylphosphatidylcholine vesicles, associated with amino acid substitution and N-terminal conjugation of the sequences with short fatty acids (8 and 12 carbon atoms). Fatty acid conjugation of peptides with low antimicrobial activity resulted in lipopeptides with improved activity against strains of Staphylococcus aureus and Listeria monocytogenes. The length of the fatty acid determined the bacterial specificity, and the conjugation with n-octanoic acid yielded the most active analog (C8-CT) against Staphylococcus aureus strain (MIC: 1.0μm) while the conjugation with n-dodecanoic acid (C12-CT) was optimal for Listeria monocytogenes strain (MIC: 2.0μm). In contrast, the substitution of Phe by Trp had an unfavorable effect on the antimicrobial activity. Hemolysis tests and membrane interaction studies with dipalmitoylphosphatidylcholine-polydiacetylene vesicles showed that lipopeptides interact to a greater extent with both biological and biomimetic membranes. Also, a good correlation was found between antimicrobial activity against Staphylococcus aureus strain and % colorimetric response values with dipalmitoylphosphatidylglycerol-polydiacetylene vesicles. Fatty acid acylated and substituted analogs of CT (GATAIKQVKKLFKKKGG), a sequence derived from region 6-22 of Plantaricin 149 were prepared with the aim to study their biological properties and the interaction with phospholipid- polydiacetylene vesicles.
Fil: Siano, Alvaro Sebastían. Universidad Nacional del Litoral; Argentina
Fil: Húmpola, Maria Veronica. Universidad Nacional del Litoral; Argentina
Fil: Rey, María Carolina. Universidad Nacional del Litoral; Argentina
Fil: Simonetta, Arturo Carlos. Universidad Nacional del Litoral; Argentina
Fil: Tonarelli, Georgina Guadalupe. Universidad Nacional del Litoral; Argentina
Materia
ANTIMICROBIAL ACTIVITY
BIOASSAYS
HEMOLYSIS
LIPOSOMES
PDA
PEPTIDES
PHOSPHOLIPIDS
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:11336/100838
Acceder
id CONICETDig_9f15fc77088272056ef6d430f40d3239
oai_identifier_str oai:ri.conicet.gov.ar:11336/100838
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Interaction of acylated and substituted antimicrobial peptide analogs with phospholipid-polydiacetylene vesicles. Correlation with their biological propertiesSiano, Alvaro SebastíanHúmpola, Maria VeronicaRey, María CarolinaSimonetta, Arturo CarlosTonarelli, Georgina GuadalupeANTIMICROBIAL ACTIVITYBIOASSAYSHEMOLYSISLIPOSOMESPDAPEPTIDESPHOSPHOLIPIDShttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1A series of peptide analogs based on region 6-22 of Plantaricin 149 sequence were synthesized. The interaction between these analogs and phospholipid-polydiacetylene vesicles was investigated to evaluate the ability of the bioassay to detect differences in the interaction of the peptides with dipalmitoylphosphatidylglycerol and dipalmitoylphosphatidylcholine vesicles, associated with amino acid substitution and N-terminal conjugation of the sequences with short fatty acids (8 and 12 carbon atoms). Fatty acid conjugation of peptides with low antimicrobial activity resulted in lipopeptides with improved activity against strains of Staphylococcus aureus and Listeria monocytogenes. The length of the fatty acid determined the bacterial specificity, and the conjugation with n-octanoic acid yielded the most active analog (C8-CT) against Staphylococcus aureus strain (MIC: 1.0μm) while the conjugation with n-dodecanoic acid (C12-CT) was optimal for Listeria monocytogenes strain (MIC: 2.0μm). In contrast, the substitution of Phe by Trp had an unfavorable effect on the antimicrobial activity. Hemolysis tests and membrane interaction studies with dipalmitoylphosphatidylcholine-polydiacetylene vesicles showed that lipopeptides interact to a greater extent with both biological and biomimetic membranes. Also, a good correlation was found between antimicrobial activity against Staphylococcus aureus strain and % colorimetric response values with dipalmitoylphosphatidylglycerol-polydiacetylene vesicles. Fatty acid acylated and substituted analogs of CT (GATAIKQVKKLFKKKGG), a sequence derived from region 6-22 of Plantaricin 149 were prepared with the aim to study their biological properties and the interaction with phospholipid- polydiacetylene vesicles.Fil: Siano, Alvaro Sebastían. Universidad Nacional del Litoral; ArgentinaFil: Húmpola, Maria Veronica. Universidad Nacional del Litoral; ArgentinaFil: Rey, María Carolina. Universidad Nacional del Litoral; ArgentinaFil: Simonetta, Arturo Carlos. Universidad Nacional del Litoral; ArgentinaFil: Tonarelli, Georgina Guadalupe. Universidad Nacional del Litoral; ArgentinaWiley Blackwell Publishing, Inc2011-07info: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/11336/100838Siano, Alvaro Sebastían; Húmpola, Maria Veronica; Rey, María Carolina; Simonetta, Arturo Carlos; Tonarelli, Georgina Guadalupe; Interaction of acylated and substituted antimicrobial peptide analogs with phospholipid-polydiacetylene vesicles. Correlation with their biological properties; Wiley Blackwell Publishing, Inc; Chemical Biology & Drug Design; 78; 1; 7-2011; 85-931747-0277CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/j.1747-0285.2011.01099.x/pdfinfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1747-0285.2011.01099.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:41:31Zoai:ri.conicet.gov.ar:11336/100838instacron: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 10:41:31.346CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Interaction of acylated and substituted antimicrobial peptide analogs with phospholipid-polydiacetylene vesicles. Correlation with their biological properties
title Interaction of acylated and substituted antimicrobial peptide analogs with phospholipid-polydiacetylene vesicles. Correlation with their biological properties
spellingShingle Interaction of acylated and substituted antimicrobial peptide analogs with phospholipid-polydiacetylene vesicles. Correlation with their biological properties
Siano, Alvaro Sebastían
ANTIMICROBIAL ACTIVITY
BIOASSAYS
HEMOLYSIS
LIPOSOMES
PDA
PEPTIDES
PHOSPHOLIPIDS
title_short Interaction of acylated and substituted antimicrobial peptide analogs with phospholipid-polydiacetylene vesicles. Correlation with their biological properties
title_full Interaction of acylated and substituted antimicrobial peptide analogs with phospholipid-polydiacetylene vesicles. Correlation with their biological properties
title_fullStr Interaction of acylated and substituted antimicrobial peptide analogs with phospholipid-polydiacetylene vesicles. Correlation with their biological properties
title_full_unstemmed Interaction of acylated and substituted antimicrobial peptide analogs with phospholipid-polydiacetylene vesicles. Correlation with their biological properties
title_sort Interaction of acylated and substituted antimicrobial peptide analogs with phospholipid-polydiacetylene vesicles. Correlation with their biological properties
dc.creator.none.fl_str_mv Siano, Alvaro Sebastían
Húmpola, Maria Veronica
Rey, María Carolina
Simonetta, Arturo Carlos
Tonarelli, Georgina Guadalupe
author Siano, Alvaro Sebastían
author_facet Siano, Alvaro Sebastían
Húmpola, Maria Veronica
Rey, María Carolina
Simonetta, Arturo Carlos
Tonarelli, Georgina Guadalupe
author_role author
author2 Húmpola, Maria Veronica
Rey, María Carolina
Simonetta, Arturo Carlos
Tonarelli, Georgina Guadalupe
author2_role author
author
author
author
dc.subject.none.fl_str_mv ANTIMICROBIAL ACTIVITY
BIOASSAYS
HEMOLYSIS
LIPOSOMES
PDA
PEPTIDES
PHOSPHOLIPIDS
topic ANTIMICROBIAL ACTIVITY
BIOASSAYS
HEMOLYSIS
LIPOSOMES
PDA
PEPTIDES
PHOSPHOLIPIDS
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 series of peptide analogs based on region 6-22 of Plantaricin 149 sequence were synthesized. The interaction between these analogs and phospholipid-polydiacetylene vesicles was investigated to evaluate the ability of the bioassay to detect differences in the interaction of the peptides with dipalmitoylphosphatidylglycerol and dipalmitoylphosphatidylcholine vesicles, associated with amino acid substitution and N-terminal conjugation of the sequences with short fatty acids (8 and 12 carbon atoms). Fatty acid conjugation of peptides with low antimicrobial activity resulted in lipopeptides with improved activity against strains of Staphylococcus aureus and Listeria monocytogenes. The length of the fatty acid determined the bacterial specificity, and the conjugation with n-octanoic acid yielded the most active analog (C8-CT) against Staphylococcus aureus strain (MIC: 1.0μm) while the conjugation with n-dodecanoic acid (C12-CT) was optimal for Listeria monocytogenes strain (MIC: 2.0μm). In contrast, the substitution of Phe by Trp had an unfavorable effect on the antimicrobial activity. Hemolysis tests and membrane interaction studies with dipalmitoylphosphatidylcholine-polydiacetylene vesicles showed that lipopeptides interact to a greater extent with both biological and biomimetic membranes. Also, a good correlation was found between antimicrobial activity against Staphylococcus aureus strain and % colorimetric response values with dipalmitoylphosphatidylglycerol-polydiacetylene vesicles. Fatty acid acylated and substituted analogs of CT (GATAIKQVKKLFKKKGG), a sequence derived from region 6-22 of Plantaricin 149 were prepared with the aim to study their biological properties and the interaction with phospholipid- polydiacetylene vesicles.
Fil: Siano, Alvaro Sebastían. Universidad Nacional del Litoral; Argentina
Fil: Húmpola, Maria Veronica. Universidad Nacional del Litoral; Argentina
Fil: Rey, María Carolina. Universidad Nacional del Litoral; Argentina
Fil: Simonetta, Arturo Carlos. Universidad Nacional del Litoral; Argentina
Fil: Tonarelli, Georgina Guadalupe. Universidad Nacional del Litoral; Argentina
description A series of peptide analogs based on region 6-22 of Plantaricin 149 sequence were synthesized. The interaction between these analogs and phospholipid-polydiacetylene vesicles was investigated to evaluate the ability of the bioassay to detect differences in the interaction of the peptides with dipalmitoylphosphatidylglycerol and dipalmitoylphosphatidylcholine vesicles, associated with amino acid substitution and N-terminal conjugation of the sequences with short fatty acids (8 and 12 carbon atoms). Fatty acid conjugation of peptides with low antimicrobial activity resulted in lipopeptides with improved activity against strains of Staphylococcus aureus and Listeria monocytogenes. The length of the fatty acid determined the bacterial specificity, and the conjugation with n-octanoic acid yielded the most active analog (C8-CT) against Staphylococcus aureus strain (MIC: 1.0μm) while the conjugation with n-dodecanoic acid (C12-CT) was optimal for Listeria monocytogenes strain (MIC: 2.0μm). In contrast, the substitution of Phe by Trp had an unfavorable effect on the antimicrobial activity. Hemolysis tests and membrane interaction studies with dipalmitoylphosphatidylcholine-polydiacetylene vesicles showed that lipopeptides interact to a greater extent with both biological and biomimetic membranes. Also, a good correlation was found between antimicrobial activity against Staphylococcus aureus strain and % colorimetric response values with dipalmitoylphosphatidylglycerol-polydiacetylene vesicles. Fatty acid acylated and substituted analogs of CT (GATAIKQVKKLFKKKGG), a sequence derived from region 6-22 of Plantaricin 149 were prepared with the aim to study their biological properties and the interaction with phospholipid- polydiacetylene vesicles.
publishDate 2011
dc.date.none.fl_str_mv 2011-07
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/11336/100838
Siano, Alvaro Sebastían; Húmpola, Maria Veronica; Rey, María Carolina; Simonetta, Arturo Carlos; Tonarelli, Georgina Guadalupe; Interaction of acylated and substituted antimicrobial peptide analogs with phospholipid-polydiacetylene vesicles. Correlation with their biological properties; Wiley Blackwell Publishing, Inc; Chemical Biology & Drug Design; 78; 1; 7-2011; 85-93
1747-0277
CONICET Digital
CONICET
url http://hdl.handle.net/11336/100838
identifier_str_mv Siano, Alvaro Sebastían; Húmpola, Maria Veronica; Rey, María Carolina; Simonetta, Arturo Carlos; Tonarelli, Georgina Guadalupe; Interaction of acylated and substituted antimicrobial peptide analogs with phospholipid-polydiacetylene vesicles. Correlation with their biological properties; Wiley Blackwell Publishing, Inc; Chemical Biology & Drug Design; 78; 1; 7-2011; 85-93
1747-0277
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/j.1747-0285.2011.01099.x/pdf
info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1747-0285.2011.01099.x
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 Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
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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