Interaction of cationic surfactants with DPPC membranes: effect of a novel Nα -benzoylated arginine-based compound

Autores
Hermet, Melisa; Fait, María Elisa; Vázquez, Romina Florencia; Maté, Sabina María; Daza Millone, María Antonieta; Vela, María Elena; Garcia, María Teresa; Morcelle del Valle, Susana Raquel; Bakás, Laura Susana
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Cationic amino acid-based surfactants are known to interact with the lipid bilayer of microorganism resulting in cell death through a disruption of the membrane topology. To elucidate the interaction of a cationic surfactant synthesized in our lab, investigations involving Nα-benzoyl-arginine decyl amide (Bz-Arg-NHC₁₀), and model membranes composed by 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) were done. Bz-Arg-NHC₁₀ was able to penetrate into DPPC monolayers up to a critical pressure of 59.6 mN m−1. Differential scanning calorimetry revealed that as the concentration of Bz-Arg-NHC₁₀ increased, the main transition temperature of DPPC slightly decreased. Atomic force microscopy (AFM) in situ experiments performed on supported DPPC bilayers on mica allowed monitoring the changes induced by Bz-Arg-NHC₁₀. DPPC bilayer patches were partially removed, mainly in borders and bilayer defects for 50 µM Bz-Arg-NHC₁₀ solution. Increasing the concentration to 100 µM resulted in a complete depletion of the supported bilayers. Surface plasmon resonance (SPR) experiments, carried out with fully DPPC bilayers covered chips, showed a net increase of the SPR signal, which can be explained by Bz-Arg-NHC₁₀ adsorption. When patchy DPPC bilayers were formed on the substrate, a SPR signal net decrease was obtained, which is consistent with the phospholipids’ removal observed in the AFM images. The results obtained suggest that the presence of the benzoyl group attached to the polar head of our compound would be the responsible of the increased antimicrobial activity against gram-negative bacteria when compared with other arginine-based surfactants.
Centro de Investigación de Proteínas Vegetales
Materia
Biología
Arginine-based surfactants
Model biological membranes
DPPC bilayer
Antibacterial activity
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/142994

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network_name_str SEDICI (UNLP)
spelling Interaction of cationic surfactants with DPPC membranes: effect of a novel Nα -benzoylated arginine-based compoundHermet, MelisaFait, María ElisaVázquez, Romina FlorenciaMaté, Sabina MaríaDaza Millone, María AntonietaVela, María ElenaGarcia, María TeresaMorcelle del Valle, Susana RaquelBakás, Laura SusanaBiologíaArginine-based surfactantsModel biological membranesDPPC bilayerAntibacterial activityCationic amino acid-based surfactants are known to interact with the lipid bilayer of microorganism resulting in cell death through a disruption of the membrane topology. To elucidate the interaction of a cationic surfactant synthesized in our lab, investigations involving Nα-benzoyl-arginine decyl amide (Bz-Arg-NHC₁₀), and model membranes composed by 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) were done. Bz-Arg-NHC₁₀ was able to penetrate into DPPC monolayers up to a critical pressure of 59.6 mN m−1. Differential scanning calorimetry revealed that as the concentration of Bz-Arg-NHC₁₀ increased, the main transition temperature of DPPC slightly decreased. Atomic force microscopy (AFM) in situ experiments performed on supported DPPC bilayers on mica allowed monitoring the changes induced by Bz-Arg-NHC₁₀. DPPC bilayer patches were partially removed, mainly in borders and bilayer defects for 50 µM Bz-Arg-NHC₁₀ solution. Increasing the concentration to 100 µM resulted in a complete depletion of the supported bilayers. Surface plasmon resonance (SPR) experiments, carried out with fully DPPC bilayers covered chips, showed a net increase of the SPR signal, which can be explained by Bz-Arg-NHC₁₀ adsorption. When patchy DPPC bilayers were formed on the substrate, a SPR signal net decrease was obtained, which is consistent with the phospholipids’ removal observed in the AFM images. The results obtained suggest that the presence of the benzoyl group attached to the polar head of our compound would be the responsible of the increased antimicrobial activity against gram-negative bacteria when compared with other arginine-based surfactants.Centro de Investigación de Proteínas Vegetales2021-03-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf609-619http://sedici.unlp.edu.ar/handle/10915/142994enginfo:eu-repo/semantics/altIdentifier/issn/1438-2199info:eu-repo/semantics/altIdentifier/issn/0939-4451info:eu-repo/semantics/altIdentifier/doi/10.1007/s00726-021-02964-2info:eu-repo/semantics/altIdentifier/pmid/33710434info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:32:32Zoai:sedici.unlp.edu.ar:10915/142994Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:32:33.017SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Interaction of cationic surfactants with DPPC membranes: effect of a novel Nα -benzoylated arginine-based compound
title Interaction of cationic surfactants with DPPC membranes: effect of a novel Nα -benzoylated arginine-based compound
spellingShingle Interaction of cationic surfactants with DPPC membranes: effect of a novel Nα -benzoylated arginine-based compound
Hermet, Melisa
Biología
Arginine-based surfactants
Model biological membranes
DPPC bilayer
Antibacterial activity
title_short Interaction of cationic surfactants with DPPC membranes: effect of a novel Nα -benzoylated arginine-based compound
title_full Interaction of cationic surfactants with DPPC membranes: effect of a novel Nα -benzoylated arginine-based compound
title_fullStr Interaction of cationic surfactants with DPPC membranes: effect of a novel Nα -benzoylated arginine-based compound
title_full_unstemmed Interaction of cationic surfactants with DPPC membranes: effect of a novel Nα -benzoylated arginine-based compound
title_sort Interaction of cationic surfactants with DPPC membranes: effect of a novel Nα -benzoylated arginine-based compound
dc.creator.none.fl_str_mv Hermet, Melisa
Fait, María Elisa
Vázquez, Romina Florencia
Maté, Sabina María
Daza Millone, María Antonieta
Vela, María Elena
Garcia, María Teresa
Morcelle del Valle, Susana Raquel
Bakás, Laura Susana
author Hermet, Melisa
author_facet Hermet, Melisa
Fait, María Elisa
Vázquez, Romina Florencia
Maté, Sabina María
Daza Millone, María Antonieta
Vela, María Elena
Garcia, María Teresa
Morcelle del Valle, Susana Raquel
Bakás, Laura Susana
author_role author
author2 Fait, María Elisa
Vázquez, Romina Florencia
Maté, Sabina María
Daza Millone, María Antonieta
Vela, María Elena
Garcia, María Teresa
Morcelle del Valle, Susana Raquel
Bakás, Laura Susana
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Biología
Arginine-based surfactants
Model biological membranes
DPPC bilayer
Antibacterial activity
topic Biología
Arginine-based surfactants
Model biological membranes
DPPC bilayer
Antibacterial activity
dc.description.none.fl_txt_mv Cationic amino acid-based surfactants are known to interact with the lipid bilayer of microorganism resulting in cell death through a disruption of the membrane topology. To elucidate the interaction of a cationic surfactant synthesized in our lab, investigations involving Nα-benzoyl-arginine decyl amide (Bz-Arg-NHC₁₀), and model membranes composed by 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) were done. Bz-Arg-NHC₁₀ was able to penetrate into DPPC monolayers up to a critical pressure of 59.6 mN m−1. Differential scanning calorimetry revealed that as the concentration of Bz-Arg-NHC₁₀ increased, the main transition temperature of DPPC slightly decreased. Atomic force microscopy (AFM) in situ experiments performed on supported DPPC bilayers on mica allowed monitoring the changes induced by Bz-Arg-NHC₁₀. DPPC bilayer patches were partially removed, mainly in borders and bilayer defects for 50 µM Bz-Arg-NHC₁₀ solution. Increasing the concentration to 100 µM resulted in a complete depletion of the supported bilayers. Surface plasmon resonance (SPR) experiments, carried out with fully DPPC bilayers covered chips, showed a net increase of the SPR signal, which can be explained by Bz-Arg-NHC₁₀ adsorption. When patchy DPPC bilayers were formed on the substrate, a SPR signal net decrease was obtained, which is consistent with the phospholipids’ removal observed in the AFM images. The results obtained suggest that the presence of the benzoyl group attached to the polar head of our compound would be the responsible of the increased antimicrobial activity against gram-negative bacteria when compared with other arginine-based surfactants.
Centro de Investigación de Proteínas Vegetales
description Cationic amino acid-based surfactants are known to interact with the lipid bilayer of microorganism resulting in cell death through a disruption of the membrane topology. To elucidate the interaction of a cationic surfactant synthesized in our lab, investigations involving Nα-benzoyl-arginine decyl amide (Bz-Arg-NHC₁₀), and model membranes composed by 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) were done. Bz-Arg-NHC₁₀ was able to penetrate into DPPC monolayers up to a critical pressure of 59.6 mN m−1. Differential scanning calorimetry revealed that as the concentration of Bz-Arg-NHC₁₀ increased, the main transition temperature of DPPC slightly decreased. Atomic force microscopy (AFM) in situ experiments performed on supported DPPC bilayers on mica allowed monitoring the changes induced by Bz-Arg-NHC₁₀. DPPC bilayer patches were partially removed, mainly in borders and bilayer defects for 50 µM Bz-Arg-NHC₁₀ solution. Increasing the concentration to 100 µM resulted in a complete depletion of the supported bilayers. Surface plasmon resonance (SPR) experiments, carried out with fully DPPC bilayers covered chips, showed a net increase of the SPR signal, which can be explained by Bz-Arg-NHC₁₀ adsorption. When patchy DPPC bilayers were formed on the substrate, a SPR signal net decrease was obtained, which is consistent with the phospholipids’ removal observed in the AFM images. The results obtained suggest that the presence of the benzoyl group attached to the polar head of our compound would be the responsible of the increased antimicrobial activity against gram-negative bacteria when compared with other arginine-based surfactants.
publishDate 2021
dc.date.none.fl_str_mv 2021-03-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/142994
url http://sedici.unlp.edu.ar/handle/10915/142994
dc.language.none.fl_str_mv eng
language eng
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info:eu-repo/semantics/altIdentifier/issn/0939-4451
info:eu-repo/semantics/altIdentifier/doi/10.1007/s00726-021-02964-2
info:eu-repo/semantics/altIdentifier/pmid/33710434
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
609-619
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
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reponame_str SEDICI (UNLP)
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repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
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