2026-04-03T23:51:04Zhttps://recercat.cat/oai/request

oai:recercat.cat:10256/279352025-12-14T23:07:26Zcom_2072_452955com_2072_2054col_2072_453073

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 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 Antibiòtics pèptids Peptide antibiotics Plantes -- Malalties bacterianes Bacterial diseases of plants 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 This 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-I00 2025-01-31 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion peer-reviewed http://hdl.handle.net/10256/27935 39885784 http://hdl.handle.net/10256/27935 eng 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/ES/PEPTIDOS DIRIGIDOS A DIANAS Y PROCESOS CLAVE PARA EL CONTROL DE XYLELLA FASTIDIOSA. DISEÑO, SINTESIS Y OPTIMIZACION/ Reconeixement-NoComercial-SenseObraDerivada 4.0 Internacional http://creativecommons.org/licenses/by-nc-nd/4.0 info:eu-repo/semantics/openAccess 18 p. application/pdf Taylor and Francis 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