Covering: 2018 to Jun of 2023The efficiency of traditional antibiotics has been undermined by the proliferation of antibiotic-resistant pathogenic microorganisms, necessitating the pursuit of innovative therapeutic agents. Antimicrobial peptides (AMPs), which are part of host defence peptides found ubiquitously in nature, exhibiting a wide range of activity towards bacteria, fungi, and viruses, offer a highly promising candidate solution. The efficacy of AMPs can frequently be augmented alterations to their amino acid sequences or structural adjustments. Given the vast reservoir of marine life forms and their distinctive ecosystems, marine AMPs stand as a burgeoning focal point in the quest for alternative peptide templates extracted from natural sources. Advances in identification and characterization techniques have accelerated the discoveries of marine AMPs, thereby stimulating AMP customization, optimization, and synthesis research endeavours. This review presents an overview of recent discoveries related to the intriguing qualities of marine AMPs. Emphasis will be placed upon post-translational modifications (PTMs) of marine AMPs and how they may impact functionality and potency. Additionally, this review considers ways in which marine PTM might support larger-scale, heterologous AMP manufacturing initiatives, providing insights into translational applications of these important biomolecules.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1039/d3np00031a | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Discovery and Characterization of an Atypical Crustin Antimicrobial Peptide from .
Mar Drugs
November 2024
Guangxi Key Laboratory of Beibu Gulf Marine Biodiversity Conservation, Beibu Gulf University, Qinzhou 535011, China.
Crustins are a family of antimicrobial peptides (AMPs) that play a pivotal role in the innate immune system of crustaceans. The discovery of novel AMPs from natural sources is crucial for expanding our current database of these peptides. Here, we identified and characterized a novel member of the crustin family, named Crus-SWD1, derived from .
View Article and Find Full Text PDFAggregation-prone antimicrobial peptides target gram-negative bacterial nucleic acids and protein synthesis.
Acta Biomater
December 2024
Shenzhen Key Laboratory of Marine Bioresource and Eco-Environmental Science, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen 518060, China. Electronic address:
Article Synopsis
- Aggregation of antimicrobial peptides (AMPs) can increase their effectiveness against bacteria by disrupting their cell structures, presenting a potential solution to antibiotic resistance.
- Researchers focused on the cephalopod Octopus bimaculoides, which lacks known AMP genes, and utilized artificial intelligence to identify four aggregation-prone peptides (Oct-P1 to Oct-P4), with Oct-P2 showing a 90% reduction in bacterial viability.
- The study revealed that Oct-P2 not only penetrates bacterial cells but also interacts with DNA, hindering gene expression, thus illustrating its promise as a template for developing new antimicrobial therapies.
Identification of a novel antimicrobial peptide from amphioxus ribosomal protein L27.
Fish Shellfish Immunol
November 2024
Key Laboratory of Evolution & Marine Biodiversity (Ministry of Education), Institute of Evolution & Marine Biodiversity, College of Marine Life Sciences, Ocean University of China, Qingdao, 266003, China; Laboratory for Marine Biology and Biotechnology, Qingdao Marine Science and Technology Center, Qingdao, 266237, China. Electronic address:
Antimicrobial peptides (AMPs), derived from a variety of proteins such as ribosomal proteins, play a pivotal role in the innate immune system. However, information regarding ribosomal protein-derived AMPs is currently limited and their mechanisms of action remain poorly defined. Here we identified and characterized the antibacterial activity of amphioxus RPL27 (BjRPL27) and its core functional region located at residues 51-72 (termed BjRPL27).
View Article and Find Full Text PDFEffect of Surface-Immobilized States of Antimicrobial Peptides on Their Ability to Disrupt Bacterial Cell Membrane Structure.
J Funct Biomater
October 2024
State Key Laboratory of Maritime Technology and Safety, Wuhan University of Technology, Wuhan 430063, China.
Article Synopsis
- * Molecular dynamics simulations showed that AMPs can disrupt bacterial cell membranes by changing their thickness and curvature, with varying effects based on how the AMPs are attached to surfaces.
- * The study found that immobilized AMPs' ability to disrupt membranes relies on electrostatic interactions, which could help design more effective and stable AMP surfaces for better antimicrobial performance.
Unveiling Encrypted Antimicrobial Peptides from Cephalopods' Salivary Glands: A Proteolysis-Driven Virtual Approach.
ACS Omega
October 2024
CIIMAR-Centro Interdisciplinar de Investigação Marinha e Ambiental, Universidade do Porto, Terminal de Cruzeiros do Porto de Leixões, Av. General Norton de Matos, s/n, Porto 4450-208, Portugal.
Antimicrobial peptides (AMPs) have potential against antimicrobial resistance and serve as templates for novel therapeutic agents. While most AMP databases focus on terrestrial eukaryotes, marine cephalopods represent a promising yet underexplored source. This study reveals the putative reservoir of AMPs encrypted within the proteomes of cephalopod salivary glands via in silico proteolysis.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!