Influence of the Nature of the Cationic Residues on the Activity of the Antimicrobial Peptides of the Lynronne Family
9 affiliations
- 1Aix Marseille Univ, CNRS, Centrale Med, iSm2 Marseille France
- 2Unité Bactériologie, Département Microbiologie et Maladies Infectieuses, UMR‐MD1‐Inserm 1261 Institut de Recherche Biomédicale des Armées (IRBA) ‐ Brétigny‐Sur‐Orge France
- 3Aix‐Marseille Univ, CNRS, LISM UMR7255 Marseille France
- 4Aix Marseille Univ, CNRS, Centrale Med, FSCM Marseille France
- 5Institute for Global Food Security, School of Biological Sciences Queen's University Belfast Belfast UK
- 6Yelen Analytics Ensues La Redonne France
- 7Departamento de Ciência da Compuagomes@ação Instituto Federal de Brasília, Campus Taguatinga Brasília Brazil
- 8S‐Inova Biotech, Graduate Program in Biotechnology Dom Bosco Catholic University Campo Grande MS Brazil
- 9Center for Proteomic and Biochemical Analysis, Graduate Program in Genomic Sciences and Biotechnology Catholic University of Brasília Brasília DF Brazil
Abstract
Most antimicrobial peptides (AMPs) are cationic, with positively charged amino acid residues (i.e., arginine, lysine, and/or histidine) being responsible for their selective interaction with bacteria. In the present study, we investigated the influence of the nature of cationic residues taking the Lynronnes peptides as models. Derivatives were designed and synthetized with substitutions of the type of cationic residues present. All derivatives and parental peptides were studied in terms of secondary structure, antimicrobial activity, anti‐biofilm activity, mechanism of action, and in vitro toxicity. All‐His peptides were found inactive, whereas all‐Lys variants showed the highest potency against Gram‐negative strains, particularly against E. coli . All‐Arg analogues were more active against Gram‐positive strains with enhanced stability under salt or serum conditions but were also more hemolytic. Mechanistic studies revealed that the peptides act by membrane permeabilization. Finally, Lynronne‐3 and its all‐Lys derivative proved the most effective in both the prevention and eradication of biofilms. These findings confirm that the type of cationic residue present in AMPs affects their activity, toxicity, and sensitivity to host factors, with different effects depending on the rest of the amino acid sequence, Lys‐substitution emerging as a promising strategy in the case of Lynronnes for targeting E. coli .
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BibTeX
@article{reinbold2026influence,
title = {{Influence of the Nature of the Cationic Residues on the Activity of the Antimicrobial Peptides of the Lynronne Family}},
author = {Alexis Reinbold and Maxime Gâchon and Jean‐François Cavalier and Laure Genet and Sophie Guillier and Mathilde Lescat and Muriel Serradeil‐Albalat and Linda B. Oyama and Cendrine Nicoletti and Sharon A. Huws and Nicolas Vidal and Fabiano Cavalcanti Fernandes and Andreia Gomes Martins and Stéphane Canaan and Octávio Luiz Franco and Sophie Tronnet and Olga Iranzo and Marc Maresca},
journal = {Journal of Peptide Science},
year = {2026},
month = nov,
doi = {10.1002/psc.70146},
url = {https://doi.org/10.1002/psc.70146},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Influence of the Nature of the Cationic Residues on the Activity of the Antimicrobial Peptides of the Lynronne Family
AU - Alexis Reinbold
AU - Maxime Gâchon
AU - Jean‐François Cavalier
AU - Laure Genet
AU - Sophie Guillier
AU - Mathilde Lescat
AU - Muriel Serradeil‐Albalat
AU - Linda B. Oyama
AU - Cendrine Nicoletti
AU - Sharon A. Huws
AU - Nicolas Vidal
AU - Fabiano Cavalcanti Fernandes
AU - Andreia Gomes Martins
AU - Stéphane Canaan
AU - Octávio Luiz Franco
AU - Sophie Tronnet
AU - Olga Iranzo
AU - Marc Maresca
PY - 2026
DA - 2026/11/03
JO - Journal of Peptide Science
DO - 10.1002/psc.70146
UR - https://doi.org/10.1002/psc.70146
AB - Most antimicrobial peptides (AMPs) are cationic, with positively charged amino acid residues (i.e., arginine, lysine, and/or histidine) being responsible for their selective interaction with bacteria. In the present study, we investigated the influence of the nature of cationic residues taking the Lynronnes peptides as models. Derivatives were designed and synthetized with substitutions of the type of cationic residues present. All derivatives and parental peptides were studied in terms of secondary structure, antimicrobial activity, anti‐biofilm activity, mechanism of action, and in vitro toxicity. All‐His peptides were found inactive, whereas all‐Lys variants showed the highest potency against Gram‐negative strains, particularly against E. coli . All‐Arg analogues were more active against Gram‐positive strains with enhanced stability under salt or serum conditions but were also more hemolytic. Mechanistic studies revealed that the peptides act by membrane permeabilization. Finally, Lynronne‐3 and its all‐Lys derivative proved the most effective in both the prevention and eradication of biofilms. These findings confirm that the type of cationic residue present in AMPs affects their activity, toxicity, and sensitivity to host factors, with different effects depending on the rest of the amino acid sequence, Lys‐substitution emerging as a promising strategy in the case of Lynronnes for targeting E. coli .
SN - 1075-2617
SN - 1099-1387
ER -