This review assesses the antiviral capabilities of antimicrobial peptides (AMPs) against SARS-CoV-2 and other respiratory viruses, focussing on their therapeutic potential. AMPs, derived from natural sources, exhibit promising antiviral properties by disrupting viral membranes, inhibiting viral entry, and modulating host immune responses. Preclinical studies demonstrate that peptides such as defensins, cathelicidins, and lactoferrin can effectively reduce SARS-CoV-2 replication and inhibit viral spread. In addition, AMPs have shown potential in enhancing the host's antiviral immunity. Despite these promising outcomes, several challenges require assessments before transforming into clinical translation. Several issues related to peptide stability, cytotoxicity, and efficient delivery systems pose significant limitations to their therapeutic application. Recent advancements in peptide engineering, nanotechnology-based delivery systems, and peptide conjugation strategies have improved AMPs stability and bioavailability; however, further optimization is essential. Moreover, whilst AMPs are safe, their effects on host cells and tissues need a thorough investigation to minimise potential adverse reactions. This review concludes that whilst AMPs present a promising route for antiviral therapies, particularly in targeting SARS-CoV-2, extensive clinical trials and additional studies are required to overcome current limitations. Future research should focus on developing more stable, less toxic AMPs formulations with enhanced delivery mechanisms, aiming to integrate AMPs into viable therapeutic options for respiratory viral diseases, including COVID-19 and other emerging infections.
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http://dx.doi.org/10.1007/s13205-024-04184-3 | DOI Listing |
3 Biotech
February 2025
Shree. S. K. Patel College of Pharmaceutical Education and Research, Ganpat University, Kherva, Gujarat 384012 India.
This review assesses the antiviral capabilities of antimicrobial peptides (AMPs) against SARS-CoV-2 and other respiratory viruses, focussing on their therapeutic potential. AMPs, derived from natural sources, exhibit promising antiviral properties by disrupting viral membranes, inhibiting viral entry, and modulating host immune responses. Preclinical studies demonstrate that peptides such as defensins, cathelicidins, and lactoferrin can effectively reduce SARS-CoV-2 replication and inhibit viral spread.
View Article and Find Full Text PDFSci Rep
January 2025
Laboratory of Extremophiles Biology, Department of Microbiology, Faculty of Biology, University of Gdansk, Wita Stwosza 59, Gdansk, 80-308, Poland.
In this study, we evaluated the combined effect between MLE-15, a modular lytic enzyme composed of four building blocks, and reline, a natural deep eutectic solvent. The bioinformatic analysis allowed us to determine the spatial architecture of MLE-15, whose components were bactericidal peptide cecropin A connected via a flexible linker to the cell wall binding domain (CBD) of mesophilic 201ϕ2 - 1 endolysin and catalytic domain (EAD) of highly thermostable Ph2119 endolysin. The modular enzyme showed high thermostability with the melting temperature of 93.
View Article and Find Full Text PDFSci Data
January 2025
Plant Science Program, Biological and Environmental Science and Engineering Division (BESE), King Abdullah University of Science and Technology (KAUST), 23955-6900, Thuwal, Saudi Arabia.
The pomegranate (Punica granatum L.) is an ancient fruit-bearing tree known for its nutritional and antioxidant properties. They originated from the Middle East in regions having large farms including mountainous regions of Al-Baha in Saudi Arabia.
View Article and Find Full Text PDFJ Nat Prod
January 2025
Department of Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen 9747AG, The Netherlands.
Recent genome mining work revealed that unexplored habitats exhibit great potential for discovering new nonribosomal peptides (NRPs) and ribosomally synthesized and post-translationally modified peptides (RiPPs). Lanthipeptides are a group of RiPPs exhibiting a variety of biological functions. They are characterized by the presence of the thioether-containing bis-amino acids lanthionine and/or methyllanthionine.
View Article and Find Full Text PDFCrit Rev Food Sci Nutr
January 2025
School of Food Science and Engineering, Hainan University, Haikou, P.R. China.
Seaweed, a promising source of nutritional proteins, including protein hydrolysates, bioactive peptides, phycobiliproteins, and lectins with multi-biological activities. Seaweeds-derived proteins and peptides have attracted increasing interest for their potential applications in dietary supplements, functional foods, and pharmaceuticals industries. This work aims to comprehensively review the preparation methods and virtual screening strategies for seaweed-derived functional peptides.
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