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
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/142994
Ver los metadatos del registro completo
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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 |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/issn/1438-2199 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) |
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application/pdf 609-619 |
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