Elastic behavior of model membranes with antimicrobial peptides depends on lipid specificity and d-enantiomers

Autores
Kumagai, Akari; Dupuy, Fernando Gabriel; Arsov, Zoran; Elhady, Yasmene; Moody, Diamond; Erns, Robert; Deslouches, Berthony; Montelaro, Ronald; Di, Yuanpu Peter; Tristram-Nagle, Stephanie
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In an effort to provide new treatments for the global crisis of bacterial resistance to current antibiotics, we have used a rational approach to design several new antimicrobial peptides (AMPs). The present study focuses on 24-mer WLBU2 and its derivative, D8, with the amino acid sequence, RRWVRRVRRWVRRVVRVVRRWVRR. In D8, all of the valines are the Denantiomer. We use X-ray low- and wide-angle diffuse scattering data to measure elasticity and lipid chain order. We show a good correlation between in vitro bacterial killing efficiency and both bending and chain order behavior in bacterial lipid membrane mimics; our results suggest that AMP-triggered domain formation could be the mechanism of bacterial killing in both Grampositive and Gram-negative bacteria. In red blood cell lipid mimics, D8 stiffens and orders the membrane, while WLBU2 softens and disorders it, which correlate with D8’s harmless vs. WLBU2’s toxic behavior in hemolysis tests. These results suggest that elasticity and chain order behavior can be used to predict mechanisms of bactericidal action and toxicity of new AMPs.
Fil: Kumagai, Akari. University of Carnegie Mellon; Estados Unidos
Fil: Dupuy, Fernando Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet Noa Sur. Instituto Superior de Investigaciones Biológicas. Grupo de Investigación y Desarrollo del Noroeste Argentino | Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas. Grupo de Investigación y Desarrollo del Noroeste Argentino; Argentina
Fil: Arsov, Zoran. Jožef Stefan Institute; Eslovenia
Fil: Elhady, Yasmene. University of Carnegie Mellon; Estados Unidos
Fil: Moody, Diamond. University of Carnegie Mellon; Estados Unidos
Fil: Erns, Robert. University of Maryland; Estados Unidos
Fil: Deslouches, Berthony. University of Pittsburgh; Estados Unidos
Fil: Montelaro, Ronald. University of Pittsburgh; Estados Unidos
Fil: Di, Yuanpu Peter. University of Pittsburgh; Estados Unidos
Fil: Tristram-Nagle, Stephanie. University of Carnegie Mellon; Estados Unidos
Materia
ANTIMICROBIAL PEPTIDE
BACTERIAL MEMBRANE
DIFFUSE X RAY SCATTERING
ORDER
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/121563
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/121563
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Elastic behavior of model membranes with antimicrobial peptides depends on lipid specificity and d-enantiomersKumagai, AkariDupuy, Fernando GabrielArsov, ZoranElhady, YasmeneMoody, DiamondErns, RobertDeslouches, BerthonyMontelaro, RonaldDi, Yuanpu PeterTristram-Nagle, StephanieANTIMICROBIAL PEPTIDEBACTERIAL MEMBRANEDIFFUSE X RAY SCATTERINGORDERhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1In an effort to provide new treatments for the global crisis of bacterial resistance to current antibiotics, we have used a rational approach to design several new antimicrobial peptides (AMPs). The present study focuses on 24-mer WLBU2 and its derivative, D8, with the amino acid sequence, RRWVRRVRRWVRRVVRVVRRWVRR. In D8, all of the valines are the Denantiomer. We use X-ray low- and wide-angle diffuse scattering data to measure elasticity and lipid chain order. We show a good correlation between in vitro bacterial killing efficiency and both bending and chain order behavior in bacterial lipid membrane mimics; our results suggest that AMP-triggered domain formation could be the mechanism of bacterial killing in both Grampositive and Gram-negative bacteria. In red blood cell lipid mimics, D8 stiffens and orders the membrane, while WLBU2 softens and disorders it, which correlate with D8’s harmless vs. WLBU2’s toxic behavior in hemolysis tests. These results suggest that elasticity and chain order behavior can be used to predict mechanisms of bactericidal action and toxicity of new AMPs.Fil: Kumagai, Akari. University of Carnegie Mellon; Estados UnidosFil: Dupuy, Fernando Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet Noa Sur. Instituto Superior de Investigaciones Biológicas. Grupo de Investigación y Desarrollo del Noroeste Argentino | Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas. Grupo de Investigación y Desarrollo del Noroeste Argentino; ArgentinaFil: Arsov, Zoran. Jožef Stefan Institute; EsloveniaFil: Elhady, Yasmene. University of Carnegie Mellon; Estados UnidosFil: Moody, Diamond. University of Carnegie Mellon; Estados UnidosFil: Erns, Robert. University of Maryland; Estados UnidosFil: Deslouches, Berthony. University of Pittsburgh; Estados UnidosFil: Montelaro, Ronald. University of Pittsburgh; Estados UnidosFil: Di, Yuanpu Peter. University of Pittsburgh; Estados UnidosFil: Tristram-Nagle, Stephanie. University of Carnegie Mellon; Estados UnidosRoyal Society of Chemistry2019-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/121563Kumagai, Akari; Dupuy, Fernando Gabriel; Arsov, Zoran; Elhady, Yasmene; Moody, Diamond; et al.; Elastic behavior of model membranes with antimicrobial peptides depends on lipid specificity and d-enantiomers; Royal Society of Chemistry; Soft Matter; 15; 8; 2-2019; 1860-18681744-683X1744-6848CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1039/C8SM02180Einfo:eu-repo/semantics/altIdentifier/url/https://pubs.rsc.org/en/content/articlelanding/2019/SM/C8SM02180Einfo:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7485610/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:49:43Zoai:ri.conicet.gov.ar:11336/121563instacron: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 09:49:43.37CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Elastic behavior of model membranes with antimicrobial peptides depends on lipid specificity and d-enantiomers
title Elastic behavior of model membranes with antimicrobial peptides depends on lipid specificity and d-enantiomers
spellingShingle Elastic behavior of model membranes with antimicrobial peptides depends on lipid specificity and d-enantiomers
Kumagai, Akari
ANTIMICROBIAL PEPTIDE
BACTERIAL MEMBRANE
DIFFUSE X RAY SCATTERING
ORDER
title_short Elastic behavior of model membranes with antimicrobial peptides depends on lipid specificity and d-enantiomers
title_full Elastic behavior of model membranes with antimicrobial peptides depends on lipid specificity and d-enantiomers
title_fullStr Elastic behavior of model membranes with antimicrobial peptides depends on lipid specificity and d-enantiomers
title_full_unstemmed Elastic behavior of model membranes with antimicrobial peptides depends on lipid specificity and d-enantiomers
title_sort Elastic behavior of model membranes with antimicrobial peptides depends on lipid specificity and d-enantiomers
dc.creator.none.fl_str_mv Kumagai, Akari
Dupuy, Fernando Gabriel
Arsov, Zoran
Elhady, Yasmene
Moody, Diamond
Erns, Robert
Deslouches, Berthony
Montelaro, Ronald
Di, Yuanpu Peter
Tristram-Nagle, Stephanie
author Kumagai, Akari
author_facet Kumagai, Akari
Dupuy, Fernando Gabriel
Arsov, Zoran
Elhady, Yasmene
Moody, Diamond
Erns, Robert
Deslouches, Berthony
Montelaro, Ronald
Di, Yuanpu Peter
Tristram-Nagle, Stephanie
author_role author
author2 Dupuy, Fernando Gabriel
Arsov, Zoran
Elhady, Yasmene
Moody, Diamond
Erns, Robert
Deslouches, Berthony
Montelaro, Ronald
Di, Yuanpu Peter
Tristram-Nagle, Stephanie
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv ANTIMICROBIAL PEPTIDE
BACTERIAL MEMBRANE
DIFFUSE X RAY SCATTERING
ORDER
topic ANTIMICROBIAL PEPTIDE
BACTERIAL MEMBRANE
DIFFUSE X RAY SCATTERING
ORDER
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv In an effort to provide new treatments for the global crisis of bacterial resistance to current antibiotics, we have used a rational approach to design several new antimicrobial peptides (AMPs). The present study focuses on 24-mer WLBU2 and its derivative, D8, with the amino acid sequence, RRWVRRVRRWVRRVVRVVRRWVRR. In D8, all of the valines are the Denantiomer. We use X-ray low- and wide-angle diffuse scattering data to measure elasticity and lipid chain order. We show a good correlation between in vitro bacterial killing efficiency and both bending and chain order behavior in bacterial lipid membrane mimics; our results suggest that AMP-triggered domain formation could be the mechanism of bacterial killing in both Grampositive and Gram-negative bacteria. In red blood cell lipid mimics, D8 stiffens and orders the membrane, while WLBU2 softens and disorders it, which correlate with D8’s harmless vs. WLBU2’s toxic behavior in hemolysis tests. These results suggest that elasticity and chain order behavior can be used to predict mechanisms of bactericidal action and toxicity of new AMPs.
Fil: Kumagai, Akari. University of Carnegie Mellon; Estados Unidos
Fil: Dupuy, Fernando Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet Noa Sur. Instituto Superior de Investigaciones Biológicas. Grupo de Investigación y Desarrollo del Noroeste Argentino | Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas. Grupo de Investigación y Desarrollo del Noroeste Argentino; Argentina
Fil: Arsov, Zoran. Jožef Stefan Institute; Eslovenia
Fil: Elhady, Yasmene. University of Carnegie Mellon; Estados Unidos
Fil: Moody, Diamond. University of Carnegie Mellon; Estados Unidos
Fil: Erns, Robert. University of Maryland; Estados Unidos
Fil: Deslouches, Berthony. University of Pittsburgh; Estados Unidos
Fil: Montelaro, Ronald. University of Pittsburgh; Estados Unidos
Fil: Di, Yuanpu Peter. University of Pittsburgh; Estados Unidos
Fil: Tristram-Nagle, Stephanie. University of Carnegie Mellon; Estados Unidos
description In an effort to provide new treatments for the global crisis of bacterial resistance to current antibiotics, we have used a rational approach to design several new antimicrobial peptides (AMPs). The present study focuses on 24-mer WLBU2 and its derivative, D8, with the amino acid sequence, RRWVRRVRRWVRRVVRVVRRWVRR. In D8, all of the valines are the Denantiomer. We use X-ray low- and wide-angle diffuse scattering data to measure elasticity and lipid chain order. We show a good correlation between in vitro bacterial killing efficiency and both bending and chain order behavior in bacterial lipid membrane mimics; our results suggest that AMP-triggered domain formation could be the mechanism of bacterial killing in both Grampositive and Gram-negative bacteria. In red blood cell lipid mimics, D8 stiffens and orders the membrane, while WLBU2 softens and disorders it, which correlate with D8’s harmless vs. WLBU2’s toxic behavior in hemolysis tests. These results suggest that elasticity and chain order behavior can be used to predict mechanisms of bactericidal action and toxicity of new AMPs.
publishDate 2019
dc.date.none.fl_str_mv 2019-02
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/11336/121563
Kumagai, Akari; Dupuy, Fernando Gabriel; Arsov, Zoran; Elhady, Yasmene; Moody, Diamond; et al.; Elastic behavior of model membranes with antimicrobial peptides depends on lipid specificity and d-enantiomers; Royal Society of Chemistry; Soft Matter; 15; 8; 2-2019; 1860-1868
1744-683X
1744-6848
CONICET Digital
CONICET
url http://hdl.handle.net/11336/121563
identifier_str_mv Kumagai, Akari; Dupuy, Fernando Gabriel; Arsov, Zoran; Elhady, Yasmene; Moody, Diamond; et al.; Elastic behavior of model membranes with antimicrobial peptides depends on lipid specificity and d-enantiomers; Royal Society of Chemistry; Soft Matter; 15; 8; 2-2019; 1860-1868
1744-683X
1744-6848
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1039/C8SM02180E
info:eu-repo/semantics/altIdentifier/url/https://pubs.rsc.org/en/content/articlelanding/2019/SM/C8SM02180E
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7485610/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Royal Society of Chemistry
publisher.none.fl_str_mv Royal Society of Chemistry
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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