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Marine antimicrobial peptides (AMPs) are potent bioactive compounds with broad-spectrum activity against bacteria, viruses, and fungi, offering a promising alternative to traditional antibiotics. These small, cationic, and amphiphilic peptides (3-50 amino acids) are key components of marine organisms' immune defenses, adapted to harsh oceanic environments. Discovered in the 1980s, marine AMPs have garnered interest for their unique structures and potential applications in human health. However, despite the ocean's vast biodiversity, they remain underexplored compared to land-based AMPs. This review emphasizes the therapeutic potential of marine AMPs, including their modes of action, structural variety, and applications in drug development, tissue regeneration, and cancer treatment. Moreover, it discusses their antibacterial, antiviral, antifungal, and antiparasitic properties. Additionally, the review addresses strategies to enhance the therapeutic potential of marine AMPs and the challenges associated with their development. By examining the promising future of marine AMPs, this review aims to pave the way for new approaches to combat antimicrobial resistance and develop innovative treatments for various infectious diseases. The potential of marine AMPs as the "medicine bank of the new millennium" remains vast, providing a valuable resource for future drug discovery and sustainable practices across industries.
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http://dx.doi.org/10.1016/j.ijbiomac.2025.142158 | DOI Listing |
Antibiotics (Basel)
August 2025
CIISA-Center for Interdisciplinary Research in Animal Health, Faculty of Veterinary Medicine, University of Lisbon, Av. Universidade Técnica, 1300-477 Lisbon, Portugal.
The global rise in antimicrobial resistance poses a major threat to public health, with multidrug-resistant bacterial infections expected to surpass cancer in mortality by 2050. As traditional antibiotic pipelines stagnate, novel therapeutic alternatives are critically needed. Antimicrobial peptides (AMPs), particularly those derived from marine organisms, have emerged as promising antimicrobial candidates due to their broad-spectrum activity, structural diversity, and distinctive mechanisms of action.
View Article and Find Full Text PDFBiomolecules
August 2025
CIIMAR/CIMAR-Interdisciplinary Centre of Marine and Environmental Research, University of Porto, Terminal de Cruzeiros do Porto de Leixões, Av. General Norton de Matos, s/n, 4450-208 Porto, Portugal.
The white-spotted jellyfish, , is an invasive species with significant ecological and economic relevance spreading across various regions. While its ecological impact is well-documented, its molecular and biochemical characteristics remain poorly understood. In this study, we integrate proteomic data generated by LC-MS/MS with publicly available transcriptomic information to characterize , analyzing differential protein expression across three distinct tissues: oral arms, mantle, and gonads.
View Article and Find Full Text PDFMar Drugs
August 2025
College of Life Sciences and Oceanography, Shenzhen University, Shenzhen 518060, China.
The growing problem of antimicrobial resistance in aquaculture, caused by the excessive and unregulated use of antibiotics, highlights the critical necessity for developing new anti-infective solutions. Based on the characteristics of glycine-rich antimicrobial peptides (AMPs) and transcriptomic data, an antimicrobial peptide, namely Rgly1, was discovered in this study. Subsequently, the peptide was obtained through heterologous expression in , and its antibacterial spectrum was determined.
View Article and Find Full Text PDFInt J Biol Macromol
September 2025
School of Marine Sciences, Ningbo University, Ningbo 315211, China; Laboratory for Marine Biology and Biotechnology, Pilot Qingdao National Laboratory for Marine Science and Technology (Qingdao), Qingdao 266071, China.
Heat shock protein 40 (HSP40) is molecular chaperone that participates in various abiotic and biotic stress. In this study, a type III HSP40 (PtHSP40-III) that mainly expresses in the thoracic ganglion of Portunus trituberculatus is identified. Despite PtHSP40-III shows relatively lower transcriptional level in hemocyte, its transcripts could be significantly induced by Vibrio alginolyticus.
View Article and Find Full Text PDFJ Med Chem
August 2025
School of Medicine, Shanghai University, Shanghai 200444, China.
Buforin II is a broad-spectrum antimicrobial peptide (AMP) that kills bacteria by targeting intracellular nucleic acids. Unlike most membrane-acting AMPs, its unique antibacterial mechanism reduced its cytotoxicity. Nonetheless, its weak antibacterial potency and poor proteolytic stability still limit its clinical translation.
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