New short cationic antibacterial peptides. Synthesis, biological activity and mechanism of action

Autores
Lima, Beatriz Viviana; Ricci, Maria; Garro, Adriana; Juhász, Tünde; Szigyártó, Imola Csilla; Papp, Zita I.; Feresin, Gabriela Egly; Garcia de la Torre, Jose; Lopez Cascales, Jose Javier; Fülöp, Lívia; Beke-Somfai, Tamás; Enriz, Ricardo Daniel
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
We report a theoretical and experimental study on a new series of small-sized antibacterial peptides. Synthesis and bioassays for these peptides are reported here. In addition, we evaluated different physicochemical parameters that modulate antimicrobial activity (charge, secondary structure, amphipathicity, hydrophobicity and polarity). We also performed molecular dynamic simulations to assess the interaction between these peptides and their molecular target (the membrane). Biophysical characterization of the peptides was carried out with different techniques, such as circular dichroism (CD), linear dichroism (LD), infrared spectroscopy (IR), dynamic light scattering (DLS), fluorescence spectroscopy and TEM studies using model systems (liposomes) for mammalian and bacterial membranes. The results of this study allow us to draw important conclusions on three different aspects. Theoretical and experimental results indicate that small-sized peptides have a particular mechanism of action that is different to that of large peptides. These results provide additional support for a previously proposed four-step mechanism of action. The possible pharmacophoric requirement for these small-sized peptides is discussed. Furthermore, our results indicate that a net +4 charge is the adequate for 9 amino acid long peptides to produce antibacterial activity. The information reported here is very important for designing new antibacterial peptides with these structural characteristics.
Fil: Lima, Beatriz Viviana. Universidad Nacional de San Juan; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Juan; Argentina
Fil: Ricci, Maria. Természettudományi Kutatóközpont; Hungría
Fil: Garro, Adriana. Universidad Nacional de San Luis; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Fil: Juhász, Tünde. Természettudományi Kutatóközpont; Hungría
Fil: Szigyártó, Imola Csilla. Természettudományi Kutatóközpont; Hungría
Fil: Papp, Zita I.. Szegedi Tudományegyetem; Hungría
Fil: Feresin, Gabriela Egly. Universidad Nacional de San Juan; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Juan; Argentina
Fil: Garcia de la Torre, Jose. Universidad de Murcia; España
Fil: Lopez Cascales, Jose Javier. Universidad Politécnica de Cartagena; España
Fil: Fülöp, Lívia. Szegedi Tudományegyetem; Hungría
Fil: Beke-Somfai, Tamás. Természettudományi Kutatóközpont; Hungría
Fil: Enriz, Ricardo Daniel. Universidad Nacional de San Luis; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Materia
ANTIMICROBIAL PEPTIDES
MECHANISM OF ACTION
PEPTIDE BIOPHYSICAL CHARACTERIZATION
SMALL-SIZED 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:11336/181663
Acceder
id CONICETDig_ec7513259d6b350a6f20696a1999fb42
oai_identifier_str oai:ri.conicet.gov.ar:11336/181663
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling New short cationic antibacterial peptides. Synthesis, biological activity and mechanism of actionLima, Beatriz VivianaRicci, MariaGarro, AdrianaJuhász, TündeSzigyártó, Imola CsillaPapp, Zita I.Feresin, Gabriela EglyGarcia de la Torre, JoseLopez Cascales, Jose JavierFülöp, LíviaBeke-Somfai, TamásEnriz, Ricardo DanielANTIMICROBIAL PEPTIDESMECHANISM OF ACTIONPEPTIDE BIOPHYSICAL CHARACTERIZATIONSMALL-SIZED PEPTIDEShttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1We report a theoretical and experimental study on a new series of small-sized antibacterial peptides. Synthesis and bioassays for these peptides are reported here. In addition, we evaluated different physicochemical parameters that modulate antimicrobial activity (charge, secondary structure, amphipathicity, hydrophobicity and polarity). We also performed molecular dynamic simulations to assess the interaction between these peptides and their molecular target (the membrane). Biophysical characterization of the peptides was carried out with different techniques, such as circular dichroism (CD), linear dichroism (LD), infrared spectroscopy (IR), dynamic light scattering (DLS), fluorescence spectroscopy and TEM studies using model systems (liposomes) for mammalian and bacterial membranes. The results of this study allow us to draw important conclusions on three different aspects. Theoretical and experimental results indicate that small-sized peptides have a particular mechanism of action that is different to that of large peptides. These results provide additional support for a previously proposed four-step mechanism of action. The possible pharmacophoric requirement for these small-sized peptides is discussed. Furthermore, our results indicate that a net +4 charge is the adequate for 9 amino acid long peptides to produce antibacterial activity. The information reported here is very important for designing new antibacterial peptides with these structural characteristics.Fil: Lima, Beatriz Viviana. Universidad Nacional de San Juan; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Juan; ArgentinaFil: Ricci, Maria. Természettudományi Kutatóközpont; HungríaFil: Garro, Adriana. Universidad Nacional de San Luis; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; ArgentinaFil: Juhász, Tünde. Természettudományi Kutatóközpont; HungríaFil: Szigyártó, Imola Csilla. Természettudományi Kutatóközpont; HungríaFil: Papp, Zita I.. Szegedi Tudományegyetem; HungríaFil: Feresin, Gabriela Egly. Universidad Nacional de San Juan; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Juan; ArgentinaFil: Garcia de la Torre, Jose. Universidad de Murcia; EspañaFil: Lopez Cascales, Jose Javier. Universidad Politécnica de Cartagena; EspañaFil: Fülöp, Lívia. Szegedi Tudományegyetem; HungríaFil: Beke-Somfai, Tamás. Természettudományi Kutatóközpont; HungríaFil: Enriz, Ricardo Daniel. Universidad Nacional de San Luis; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; ArgentinaElsevier Science2021-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/181663Lima, Beatriz Viviana; Ricci, Maria; Garro, Adriana; Juhász, Tünde; Szigyártó, Imola Csilla; et al.; New short cationic antibacterial peptides. Synthesis, biological activity and mechanism of action; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1863; 10; 10-2021; 1-130005-2736CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2021.183665info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005273621001152info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:13:26Zoai:ri.conicet.gov.ar:11336/181663instacron: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 10:13:27.078CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv New short cationic antibacterial peptides. Synthesis, biological activity and mechanism of action
title New short cationic antibacterial peptides. Synthesis, biological activity and mechanism of action
spellingShingle New short cationic antibacterial peptides. Synthesis, biological activity and mechanism of action
Lima, Beatriz Viviana
ANTIMICROBIAL PEPTIDES
MECHANISM OF ACTION
PEPTIDE BIOPHYSICAL CHARACTERIZATION
SMALL-SIZED PEPTIDES
title_short New short cationic antibacterial peptides. Synthesis, biological activity and mechanism of action
title_full New short cationic antibacterial peptides. Synthesis, biological activity and mechanism of action
title_fullStr New short cationic antibacterial peptides. Synthesis, biological activity and mechanism of action
title_full_unstemmed New short cationic antibacterial peptides. Synthesis, biological activity and mechanism of action
title_sort New short cationic antibacterial peptides. Synthesis, biological activity and mechanism of action
dc.creator.none.fl_str_mv Lima, Beatriz Viviana
Ricci, Maria
Garro, Adriana
Juhász, Tünde
Szigyártó, Imola Csilla
Papp, Zita I.
Feresin, Gabriela Egly
Garcia de la Torre, Jose
Lopez Cascales, Jose Javier
Fülöp, Lívia
Beke-Somfai, Tamás
Enriz, Ricardo Daniel
author Lima, Beatriz Viviana
author_facet Lima, Beatriz Viviana
Ricci, Maria
Garro, Adriana
Juhász, Tünde
Szigyártó, Imola Csilla
Papp, Zita I.
Feresin, Gabriela Egly
Garcia de la Torre, Jose
Lopez Cascales, Jose Javier
Fülöp, Lívia
Beke-Somfai, Tamás
Enriz, Ricardo Daniel
author_role author
author2 Ricci, Maria
Garro, Adriana
Juhász, Tünde
Szigyártó, Imola Csilla
Papp, Zita I.
Feresin, Gabriela Egly
Garcia de la Torre, Jose
Lopez Cascales, Jose Javier
Fülöp, Lívia
Beke-Somfai, Tamás
Enriz, Ricardo Daniel
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv ANTIMICROBIAL PEPTIDES
MECHANISM OF ACTION
PEPTIDE BIOPHYSICAL CHARACTERIZATION
SMALL-SIZED PEPTIDES
topic ANTIMICROBIAL PEPTIDES
MECHANISM OF ACTION
PEPTIDE BIOPHYSICAL CHARACTERIZATION
SMALL-SIZED PEPTIDES
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv We report a theoretical and experimental study on a new series of small-sized antibacterial peptides. Synthesis and bioassays for these peptides are reported here. In addition, we evaluated different physicochemical parameters that modulate antimicrobial activity (charge, secondary structure, amphipathicity, hydrophobicity and polarity). We also performed molecular dynamic simulations to assess the interaction between these peptides and their molecular target (the membrane). Biophysical characterization of the peptides was carried out with different techniques, such as circular dichroism (CD), linear dichroism (LD), infrared spectroscopy (IR), dynamic light scattering (DLS), fluorescence spectroscopy and TEM studies using model systems (liposomes) for mammalian and bacterial membranes. The results of this study allow us to draw important conclusions on three different aspects. Theoretical and experimental results indicate that small-sized peptides have a particular mechanism of action that is different to that of large peptides. These results provide additional support for a previously proposed four-step mechanism of action. The possible pharmacophoric requirement for these small-sized peptides is discussed. Furthermore, our results indicate that a net +4 charge is the adequate for 9 amino acid long peptides to produce antibacterial activity. The information reported here is very important for designing new antibacterial peptides with these structural characteristics.
Fil: Lima, Beatriz Viviana. Universidad Nacional de San Juan; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Juan; Argentina
Fil: Ricci, Maria. Természettudományi Kutatóközpont; Hungría
Fil: Garro, Adriana. Universidad Nacional de San Luis; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Fil: Juhász, Tünde. Természettudományi Kutatóközpont; Hungría
Fil: Szigyártó, Imola Csilla. Természettudományi Kutatóközpont; Hungría
Fil: Papp, Zita I.. Szegedi Tudományegyetem; Hungría
Fil: Feresin, Gabriela Egly. Universidad Nacional de San Juan; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Juan; Argentina
Fil: Garcia de la Torre, Jose. Universidad de Murcia; España
Fil: Lopez Cascales, Jose Javier. Universidad Politécnica de Cartagena; España
Fil: Fülöp, Lívia. Szegedi Tudományegyetem; Hungría
Fil: Beke-Somfai, Tamás. Természettudományi Kutatóközpont; Hungría
Fil: Enriz, Ricardo Daniel. Universidad Nacional de San Luis; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
description We report a theoretical and experimental study on a new series of small-sized antibacterial peptides. Synthesis and bioassays for these peptides are reported here. In addition, we evaluated different physicochemical parameters that modulate antimicrobial activity (charge, secondary structure, amphipathicity, hydrophobicity and polarity). We also performed molecular dynamic simulations to assess the interaction between these peptides and their molecular target (the membrane). Biophysical characterization of the peptides was carried out with different techniques, such as circular dichroism (CD), linear dichroism (LD), infrared spectroscopy (IR), dynamic light scattering (DLS), fluorescence spectroscopy and TEM studies using model systems (liposomes) for mammalian and bacterial membranes. The results of this study allow us to draw important conclusions on three different aspects. Theoretical and experimental results indicate that small-sized peptides have a particular mechanism of action that is different to that of large peptides. These results provide additional support for a previously proposed four-step mechanism of action. The possible pharmacophoric requirement for these small-sized peptides is discussed. Furthermore, our results indicate that a net +4 charge is the adequate for 9 amino acid long peptides to produce antibacterial activity. The information reported here is very important for designing new antibacterial peptides with these structural characteristics.
publishDate 2021
dc.date.none.fl_str_mv 2021-10
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/11336/181663
Lima, Beatriz Viviana; Ricci, Maria; Garro, Adriana; Juhász, Tünde; Szigyártó, Imola Csilla; et al.; New short cationic antibacterial peptides. Synthesis, biological activity and mechanism of action; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1863; 10; 10-2021; 1-13
0005-2736
CONICET Digital
CONICET
url http://hdl.handle.net/11336/181663
identifier_str_mv Lima, Beatriz Viviana; Ricci, Maria; Garro, Adriana; Juhász, Tünde; Szigyártó, Imola Csilla; et al.; New short cationic antibacterial peptides. Synthesis, biological activity and mechanism of action; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1863; 10; 10-2021; 1-13
0005-2736
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2021.183665
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005273621001152
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 Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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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