Structure-activity relationship of peptide conjugates derived from BP100 and insights into their interactions with lipid membranes by NMR and MD simulations

Antimicrobial and plant defence elicitor peptides have received attention on last decades as novel tools to combat bacterial plant diseases. We previously reported a library of peptide conjugates resulting from the combination of an antimicrobial peptide (BP16, BP143, BP387 or BP475) and a plant def...

Descripción completa

Detalles Bibliográficos
Autores: Riesco-Llach, Gerard, Oliveras Rovira, Àngel, Gil Caballero, Sergi, Badosa Romañó, Esther, Bonaterra i Carreras, Anna, Montesinos Seguí, Emilio, Feixas Geronès, Ferran, Planas i Grabuleda, Marta, Feliu Soley, Lidia
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2025
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:10256/27935
Acceso en línea:http://hdl.handle.net/10256/27935
Access Level:acceso abierto
Palabra clave:Antibiòtics pèptids
Peptide antibiotics
Plantes -- Malalties bacterianes
Bacterial diseases of plants
id ES_3f8ea7b8a2fcef602d70b2d035d61528
oai_identifier_str oai:recercat.cat:10256/27935
network_acronym_str ES
network_name_str España
repository_id_str
spelling Structure-activity relationship of peptide conjugates derived from BP100 and insights into their interactions with lipid membranes by NMR and MD simulationsRiesco-Llach, GerardOliveras Rovira, ÀngelGil Caballero, SergiBadosa Romañó, EstherBonaterra i Carreras, AnnaMontesinos Seguí, EmilioFeixas Geronès, FerranPlanas i Grabuleda, MartaFeliu Soley, LidiaAntibiòtics pèptidsPeptide antibioticsPlantes -- Malalties bacterianesBacterial diseases of plantsAntimicrobial and plant defence elicitor peptides have received attention on last decades as novel tools to combat bacterial plant diseases. We previously reported a library of peptide conjugates resulting from the combination of an antimicrobial peptide (BP16, BP143, BP387 or BP475) and a plant defence elicitor sequence (flg15, BP13, Pep13 or PIP1). From this library, we selected a set of 14 peptide conjugates including both highly and poorly active sequences and we performed a structureactivity relationship study by NMR and MD simulations. Analysis of their structure by NMR in 30% TFE-d3 and in zwitterionic DPC-d38 and anionic SDS-d25 micelles showed that the presence of an a-helix fragment together with a flexible random coil can be related to a high antibacterial activity and a low hemolysis. In contrast, the sequences with a rigid a-helix structure were low active and highly hemolytic. PRE-NMR experiments in presence of MnCl2 and 16-DSA revealed that the highly active peptides flg15-BP475 and BP100-Pep13 interacted stronger with DPC-d38 micelles than the low active peptide BP13-BP16. In the two former sequences this interaction took place through the a-helix region. From GaMD simulations of BP100-Pep13 conducted in membranes composed of anionic DPPG lipids, after its electrostatic interaction, the peptide flipped and the hydrophobic residues were faced to the membrane triggering its insertion and also causing membrane thinning. Thus, the flexibility and moderate cationicity of BP100-Pep13 seem to be crucial for its biological activity. These findings can help to establish the guidelines for future rational design of BP100 derivativesThis research was funded by grants RTI2018-099410-B-C22 (MICINN/AEI/ FEDER, UE) and PID2022-140040OB-C22 (MCIN/AEI/10.13039/ 501100011033/FEDER, UE). G.R.-L. was recipient of a fellowship from the University of Girona. F.F. thanks Generalitat de Catalunya AGAUR for 2021SGR00487 and the Spanish MINECO for RYC2020-029552-I and PID2022-141676NB-I00Taylor and Francis2025info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionpeer-reviewed18 p.application/pdfhttp://hdl.handle.net/10256/27935http://hdl.handle.net/10256/27935Journal of Biomolecular Structure & Dynamics, 2025, vol. 43, núm. 17, p. 10220-10237Articles publicats (D-Q)Riesco-Llach, Gerard Oliveras Rovira, Àngel Gil Caballero, Sergi Badosa Romañó, Esther Bonaterra i Carreras, Anna Montesinos Seguí, Emilio Feixas Geronès, Ferran Planas i Grabuleda, Marta Feliu Soley, Lidia 2025 Structure-activity relationship of peptide conjugates derived from BP100 and insights into their interactions with lipid membranes by NMR and MD simulations Journal of Biomolecular Structure & Dynamics 43 17 10220 10237reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)Inglésinfo:eu-repo/semantics/altIdentifier/doi/10.1080/07391102.2025.2458328info:eu-repo/semantics/altIdentifier/issn/0739-1102info:eu-repo/semantics/altIdentifier/eissn/1538-0254RTI2018-099410-B-C22PEPTIDOS DIRIGIDOS A DIANAS Y PROCESOS CLAVE PARA EL CONTROL DE XYLELLA FASTIDIOSA. DISEÑO, SINTESIS Y OPTIMIZACIONinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/RTI2018-099410-B-C22Reconeixement-NoComercial-SenseObraDerivada 4.0 Internacionalhttp://creativecommons.org/licenses/by-nc-nd/4.0info:eu-repo/semantics/openAccessoai:recercat.cat:10256/279352026-05-29T05:05:01Z
dc.title.none.fl_str_mv Structure-activity relationship of peptide conjugates derived from BP100 and insights into their interactions with lipid membranes by NMR and MD simulations
title Structure-activity relationship of peptide conjugates derived from BP100 and insights into their interactions with lipid membranes by NMR and MD simulations
spellingShingle Structure-activity relationship of peptide conjugates derived from BP100 and insights into their interactions with lipid membranes by NMR and MD simulations
Riesco-Llach, Gerard
Antibiòtics pèptids
Peptide antibiotics
Plantes -- Malalties bacterianes
Bacterial diseases of plants
title_short Structure-activity relationship of peptide conjugates derived from BP100 and insights into their interactions with lipid membranes by NMR and MD simulations
title_full Structure-activity relationship of peptide conjugates derived from BP100 and insights into their interactions with lipid membranes by NMR and MD simulations
title_fullStr Structure-activity relationship of peptide conjugates derived from BP100 and insights into their interactions with lipid membranes by NMR and MD simulations
title_full_unstemmed Structure-activity relationship of peptide conjugates derived from BP100 and insights into their interactions with lipid membranes by NMR and MD simulations
title_sort Structure-activity relationship of peptide conjugates derived from BP100 and insights into their interactions with lipid membranes by NMR and MD simulations
dc.creator.none.fl_str_mv Riesco-Llach, Gerard
Oliveras Rovira, Àngel
Gil Caballero, Sergi
Badosa Romañó, Esther
Bonaterra i Carreras, Anna
Montesinos Seguí, Emilio
Feixas Geronès, Ferran
Planas i Grabuleda, Marta
Feliu Soley, Lidia
author Riesco-Llach, Gerard
author_facet Riesco-Llach, Gerard
Oliveras Rovira, Àngel
Gil Caballero, Sergi
Badosa Romañó, Esther
Bonaterra i Carreras, Anna
Montesinos Seguí, Emilio
Feixas Geronès, Ferran
Planas i Grabuleda, Marta
Feliu Soley, Lidia
author_role author
author2 Oliveras Rovira, Àngel
Gil Caballero, Sergi
Badosa Romañó, Esther
Bonaterra i Carreras, Anna
Montesinos Seguí, Emilio
Feixas Geronès, Ferran
Planas i Grabuleda, Marta
Feliu Soley, Lidia
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Antibiòtics pèptids
Peptide antibiotics
Plantes -- Malalties bacterianes
Bacterial diseases of plants
topic Antibiòtics pèptids
Peptide antibiotics
Plantes -- Malalties bacterianes
Bacterial diseases of plants
description Antimicrobial and plant defence elicitor peptides have received attention on last decades as novel tools to combat bacterial plant diseases. We previously reported a library of peptide conjugates resulting from the combination of an antimicrobial peptide (BP16, BP143, BP387 or BP475) and a plant defence elicitor sequence (flg15, BP13, Pep13 or PIP1). From this library, we selected a set of 14 peptide conjugates including both highly and poorly active sequences and we performed a structureactivity relationship study by NMR and MD simulations. Analysis of their structure by NMR in 30% TFE-d3 and in zwitterionic DPC-d38 and anionic SDS-d25 micelles showed that the presence of an a-helix fragment together with a flexible random coil can be related to a high antibacterial activity and a low hemolysis. In contrast, the sequences with a rigid a-helix structure were low active and highly hemolytic. PRE-NMR experiments in presence of MnCl2 and 16-DSA revealed that the highly active peptides flg15-BP475 and BP100-Pep13 interacted stronger with DPC-d38 micelles than the low active peptide BP13-BP16. In the two former sequences this interaction took place through the a-helix region. From GaMD simulations of BP100-Pep13 conducted in membranes composed of anionic DPPG lipids, after its electrostatic interaction, the peptide flipped and the hydrophobic residues were faced to the membrane triggering its insertion and also causing membrane thinning. Thus, the flexibility and moderate cationicity of BP100-Pep13 seem to be crucial for its biological activity. These findings can help to establish the guidelines for future rational design of BP100 derivatives
publishDate 2025
dc.date.none.fl_str_mv 2025
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
peer-reviewed
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10256/27935
http://hdl.handle.net/10256/27935
url http://hdl.handle.net/10256/27935
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1080/07391102.2025.2458328
info:eu-repo/semantics/altIdentifier/issn/0739-1102
info:eu-repo/semantics/altIdentifier/eissn/1538-0254
RTI2018-099410-B-C22
PEPTIDOS DIRIGIDOS A DIANAS Y PROCESOS CLAVE PARA EL CONTROL DE XYLELLA FASTIDIOSA. DISEÑO, SINTESIS Y OPTIMIZACION
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/RTI2018-099410-B-C22
dc.rights.none.fl_str_mv Reconeixement-NoComercial-SenseObraDerivada 4.0 Internacional
http://creativecommons.org/licenses/by-nc-nd/4.0

info:eu-repo/semantics/openAccess
rights_invalid_str_mv Reconeixement-NoComercial-SenseObraDerivada 4.0 Internacional
http://creativecommons.org/licenses/by-nc-nd/4.0
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 18 p.
application/pdf
dc.publisher.none.fl_str_mv Taylor and Francis
publisher.none.fl_str_mv Taylor and Francis
dc.source.none.fl_str_mv Journal of Biomolecular Structure & Dynamics, 2025, vol. 43, núm. 17, p. 10220-10237
Articles publicats (D-Q)
Riesco-Llach, Gerard Oliveras Rovira, Àngel Gil Caballero, Sergi Badosa Romañó, Esther Bonaterra i Carreras, Anna Montesinos Seguí, Emilio Feixas Geronès, Ferran Planas i Grabuleda, Marta Feliu Soley, Lidia 2025 Structure-activity relationship of peptide conjugates derived from BP100 and insights into their interactions with lipid membranes by NMR and MD simulations Journal of Biomolecular Structure & Dynamics 43 17 10220 10237
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869406648423940097
score 15,811543

Similares en LA Referencia