Evaluating Host Defense Peptides

The global antibiotic resistance crisis raises concerns about antibiotic use, and alternative strategies are urgently needed. In this context, host defense peptides (HDPs) have rapidly gained interest. However, one of the main obstacles is their production strategy. Chemical synthesis is the most wi...

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Detalles Bibliográficos
Autores: Saubi, Cristina|||0000-0002-1866-8418, Carratalá, José Vicente|||0000-0001-6950-2939, Bello Madruga, Roberto|||0009-0003-8474-3951, López-Cano, Adrià, Navarro, Susanna|||0000-0001-8160-9536, Arís i Giralt, Anna|||0000-0001-7830-888X, Garcia-Fruitos, Elena|||0000-0001-7498-4864
Tipo de recurso: artículo
Fecha de publicación:2025
País:España
Institución:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:318771
Acceso en línea:https://ddd.uab.cat/record/318771
https://dx.doi.org/urn:doi:10.3390/biom15070980
Access Level:acceso abierto
Palabra clave:Host defense peptides
Recombinant production
Concatemers
Antimicrobial activity
Lactococcus lactis
Descripción
Sumario:The global antibiotic resistance crisis raises concerns about antibiotic use, and alternative strategies are urgently needed. In this context, host defense peptides (HDPs) have rapidly gained interest. However, one of the main obstacles is their production strategy. Chemical synthesis is the most widely used, although it is not scalable and has sequence limitations. A possible alternative is recombinant production, but the strategies used so far have limited efficiency. In this study, we aim to compare the activity and main characteristics of different HDPs produced by both chemical synthesis and by recombinant production, using an approach based on tetramers to ameliorate the production process. The results obtained showed that the production of HDPs as tetrameric peptides by recombinant production in Lactococcus lactis enhanced the peptide activity, with HDPs being much more active in terms of antimicrobial activity, more structurally stable, and nanostructured. Thus, the recombinant strategy described herein, fusing four repetitions of the same peptide, can become a real alternative to produce highly active HDPs through a scalable production process.