Leptodactylus latrans amphibian skin secretions as a novel source for the isolation of antibacterial peptides

Autores
Siano, Alvaro Sebastían; Húmpola, Maria Veronica; de Oliveira, Eliandre; Albericio Palomera, Fernando; Simonetta, Arturo Carlos; Lajmanovich, Rafael Carlos; Tonarelli, Georgina Guadalupe
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Amphibians´ skin produces a diverse array of antimicrobial peptides that play a crucial role as the first line of defense against microbial invasion. Despite the immense richness of wild amphibians in Argentina, current knowledge about the presence of peptides with antimicrobial properties is limited to a only few species. Here we used LC-MS-MS to identify antimicrobial peptides with masses ranging from 1000 to 4000 Da from samples of skin secretions of Leptodactylus latrans (Anura: Leptodactylidae). Three novel amino acid sequences were selected for chemical synthesis and further studies. The three synthetic peptides, named P1-Ll-1577, P2-Ll-1298, and P3-Ll-2085, inhibited the growth of two ATCC strains, namely Escherichia coli and Staphylococcus aureus. P3-Ll-2085 was the most active peptide. In the presence of trifluoroethanol (TFE) and anionic liposomes, it adopted an amphipathic α-helical structure. P2-Ll-1298 showed slightly lower activity than P3-Ll-2085. Comparison of the MIC values of these two peptides revealed that the addition of seven amino acid residues (GLLDFLK) on the N-terminal of P2-Ll-1298 significantly improved activity against both strains. P1-Ll-1577, which remarkably is an anionic peptide, showed interesting antimicrobial activity against E. coli and S. aureus strain, showing marked membrane selectivity and non-hemolysis. Due to this, P1-L1-1577 emerges as a potential candidate for the development of new antibacterial drugs.
Fil: Siano, Alvaro Sebastían. Universidad Nacional del Litoral; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Húmpola, Maria Veronica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Litoral; Argentina
Fil: de Oliveira, Eliandre. Proteomics Platform;
Fil: Albericio Palomera, Fernando. University Of Kwazulu-natal; . Universidad de Barcelona; España. Ciber Bioingenieria, Biomateriales y Nanomedicina;
Fil: Simonetta, Arturo Carlos. Universidad Nacional del Litoral; Argentina
Fil: Lajmanovich, Rafael Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Litoral; Argentina
Fil: Tonarelli, Georgina Guadalupe. Universidad Nacional del Litoral; Argentina
Materia
ANTIMICROBIAL
FROGS
PEPTIDES
PEPTIDOMICS
SYNTHESIS
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:11336/89638
Acceder
id CONICETDig_1cb08f1fea1e7810516a1be8e9468521
oai_identifier_str oai:ri.conicet.gov.ar:11336/89638
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Leptodactylus latrans amphibian skin secretions as a novel source for the isolation of antibacterial peptidesSiano, Alvaro SebastíanHúmpola, Maria Veronicade Oliveira, EliandreAlbericio Palomera, FernandoSimonetta, Arturo CarlosLajmanovich, Rafael CarlosTonarelli, Georgina GuadalupeANTIMICROBIALFROGSPEPTIDESPEPTIDOMICSSYNTHESIShttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Amphibians´ skin produces a diverse array of antimicrobial peptides that play a crucial role as the first line of defense against microbial invasion. Despite the immense richness of wild amphibians in Argentina, current knowledge about the presence of peptides with antimicrobial properties is limited to a only few species. Here we used LC-MS-MS to identify antimicrobial peptides with masses ranging from 1000 to 4000 Da from samples of skin secretions of Leptodactylus latrans (Anura: Leptodactylidae). Three novel amino acid sequences were selected for chemical synthesis and further studies. The three synthetic peptides, named P1-Ll-1577, P2-Ll-1298, and P3-Ll-2085, inhibited the growth of two ATCC strains, namely Escherichia coli and Staphylococcus aureus. P3-Ll-2085 was the most active peptide. In the presence of trifluoroethanol (TFE) and anionic liposomes, it adopted an amphipathic α-helical structure. P2-Ll-1298 showed slightly lower activity than P3-Ll-2085. Comparison of the MIC values of these two peptides revealed that the addition of seven amino acid residues (GLLDFLK) on the N-terminal of P2-Ll-1298 significantly improved activity against both strains. P1-Ll-1577, which remarkably is an anionic peptide, showed interesting antimicrobial activity against E. coli and S. aureus strain, showing marked membrane selectivity and non-hemolysis. Due to this, P1-L1-1577 emerges as a potential candidate for the development of new antibacterial drugs.Fil: Siano, Alvaro Sebastían. Universidad Nacional del Litoral; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Húmpola, Maria Veronica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Litoral; ArgentinaFil: de Oliveira, Eliandre. Proteomics Platform;Fil: Albericio Palomera, Fernando. University Of Kwazulu-natal; . Universidad de Barcelona; España. Ciber Bioingenieria, Biomateriales y Nanomedicina;Fil: Simonetta, Arturo Carlos. Universidad Nacional del Litoral; ArgentinaFil: Lajmanovich, Rafael Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Litoral; ArgentinaFil: Tonarelli, Georgina Guadalupe. Universidad Nacional del Litoral; ArgentinaMolecular Diversity Preservation International2018-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/89638Siano, Alvaro Sebastían; Húmpola, Maria Veronica; de Oliveira, Eliandre; Albericio Palomera, Fernando; Simonetta, Arturo Carlos; et al.; Leptodactylus latrans amphibian skin secretions as a novel source for the isolation of antibacterial peptides; Molecular Diversity Preservation International; Molecules; 23; 11; 11-20181420-3049CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/1420-3049/23/11/2943info:eu-repo/semantics/altIdentifier/doi/10.3390/molecules23112943info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:46:04Zoai:ri.conicet.gov.ar:11336/89638instacron: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:34982025-09-03 09:46:04.585CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Leptodactylus latrans amphibian skin secretions as a novel source for the isolation of antibacterial peptides
title Leptodactylus latrans amphibian skin secretions as a novel source for the isolation of antibacterial peptides
spellingShingle Leptodactylus latrans amphibian skin secretions as a novel source for the isolation of antibacterial peptides
Siano, Alvaro Sebastían
ANTIMICROBIAL
FROGS
PEPTIDES
PEPTIDOMICS
SYNTHESIS
title_short Leptodactylus latrans amphibian skin secretions as a novel source for the isolation of antibacterial peptides
title_full Leptodactylus latrans amphibian skin secretions as a novel source for the isolation of antibacterial peptides
title_fullStr Leptodactylus latrans amphibian skin secretions as a novel source for the isolation of antibacterial peptides
title_full_unstemmed Leptodactylus latrans amphibian skin secretions as a novel source for the isolation of antibacterial peptides
title_sort Leptodactylus latrans amphibian skin secretions as a novel source for the isolation of antibacterial peptides
dc.creator.none.fl_str_mv Siano, Alvaro Sebastían
Húmpola, Maria Veronica
de Oliveira, Eliandre
Albericio Palomera, Fernando
Simonetta, Arturo Carlos
Lajmanovich, Rafael Carlos
Tonarelli, Georgina Guadalupe
author Siano, Alvaro Sebastían
author_facet Siano, Alvaro Sebastían
Húmpola, Maria Veronica
de Oliveira, Eliandre
Albericio Palomera, Fernando
Simonetta, Arturo Carlos
Lajmanovich, Rafael Carlos
Tonarelli, Georgina Guadalupe
author_role author
author2 Húmpola, Maria Veronica
de Oliveira, Eliandre
Albericio Palomera, Fernando
Simonetta, Arturo Carlos
Lajmanovich, Rafael Carlos
Tonarelli, Georgina Guadalupe
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv ANTIMICROBIAL
FROGS
PEPTIDES
PEPTIDOMICS
SYNTHESIS
topic ANTIMICROBIAL
FROGS
PEPTIDES
PEPTIDOMICS
SYNTHESIS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Amphibians´ skin produces a diverse array of antimicrobial peptides that play a crucial role as the first line of defense against microbial invasion. Despite the immense richness of wild amphibians in Argentina, current knowledge about the presence of peptides with antimicrobial properties is limited to a only few species. Here we used LC-MS-MS to identify antimicrobial peptides with masses ranging from 1000 to 4000 Da from samples of skin secretions of Leptodactylus latrans (Anura: Leptodactylidae). Three novel amino acid sequences were selected for chemical synthesis and further studies. The three synthetic peptides, named P1-Ll-1577, P2-Ll-1298, and P3-Ll-2085, inhibited the growth of two ATCC strains, namely Escherichia coli and Staphylococcus aureus. P3-Ll-2085 was the most active peptide. In the presence of trifluoroethanol (TFE) and anionic liposomes, it adopted an amphipathic α-helical structure. P2-Ll-1298 showed slightly lower activity than P3-Ll-2085. Comparison of the MIC values of these two peptides revealed that the addition of seven amino acid residues (GLLDFLK) on the N-terminal of P2-Ll-1298 significantly improved activity against both strains. P1-Ll-1577, which remarkably is an anionic peptide, showed interesting antimicrobial activity against E. coli and S. aureus strain, showing marked membrane selectivity and non-hemolysis. Due to this, P1-L1-1577 emerges as a potential candidate for the development of new antibacterial drugs.
Fil: Siano, Alvaro Sebastían. Universidad Nacional del Litoral; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Húmpola, Maria Veronica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Litoral; Argentina
Fil: de Oliveira, Eliandre. Proteomics Platform;
Fil: Albericio Palomera, Fernando. University Of Kwazulu-natal; . Universidad de Barcelona; España. Ciber Bioingenieria, Biomateriales y Nanomedicina;
Fil: Simonetta, Arturo Carlos. Universidad Nacional del Litoral; Argentina
Fil: Lajmanovich, Rafael Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Litoral; Argentina
Fil: Tonarelli, Georgina Guadalupe. Universidad Nacional del Litoral; Argentina
description Amphibians´ skin produces a diverse array of antimicrobial peptides that play a crucial role as the first line of defense against microbial invasion. Despite the immense richness of wild amphibians in Argentina, current knowledge about the presence of peptides with antimicrobial properties is limited to a only few species. Here we used LC-MS-MS to identify antimicrobial peptides with masses ranging from 1000 to 4000 Da from samples of skin secretions of Leptodactylus latrans (Anura: Leptodactylidae). Three novel amino acid sequences were selected for chemical synthesis and further studies. The three synthetic peptides, named P1-Ll-1577, P2-Ll-1298, and P3-Ll-2085, inhibited the growth of two ATCC strains, namely Escherichia coli and Staphylococcus aureus. P3-Ll-2085 was the most active peptide. In the presence of trifluoroethanol (TFE) and anionic liposomes, it adopted an amphipathic α-helical structure. P2-Ll-1298 showed slightly lower activity than P3-Ll-2085. Comparison of the MIC values of these two peptides revealed that the addition of seven amino acid residues (GLLDFLK) on the N-terminal of P2-Ll-1298 significantly improved activity against both strains. P1-Ll-1577, which remarkably is an anionic peptide, showed interesting antimicrobial activity against E. coli and S. aureus strain, showing marked membrane selectivity and non-hemolysis. Due to this, P1-L1-1577 emerges as a potential candidate for the development of new antibacterial drugs.
publishDate 2018
dc.date.none.fl_str_mv 2018-11
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/11336/89638
Siano, Alvaro Sebastían; Húmpola, Maria Veronica; de Oliveira, Eliandre; Albericio Palomera, Fernando; Simonetta, Arturo Carlos; et al.; Leptodactylus latrans amphibian skin secretions as a novel source for the isolation of antibacterial peptides; Molecular Diversity Preservation International; Molecules; 23; 11; 11-2018
1420-3049
CONICET Digital
CONICET
url http://hdl.handle.net/11336/89638
identifier_str_mv Siano, Alvaro Sebastían; Húmpola, Maria Veronica; de Oliveira, Eliandre; Albericio Palomera, Fernando; Simonetta, Arturo Carlos; et al.; Leptodactylus latrans amphibian skin secretions as a novel source for the isolation of antibacterial peptides; Molecular Diversity Preservation International; Molecules; 23; 11; 11-2018
1420-3049
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://www.mdpi.com/1420-3049/23/11/2943
info:eu-repo/semantics/altIdentifier/doi/10.3390/molecules23112943
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
dc.publisher.none.fl_str_mv Molecular Diversity Preservation International
publisher.none.fl_str_mv Molecular Diversity Preservation International
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
_version_ 1842268771786424320
score 13.13397

Publicaciones similares