Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
Antibacterial resistance has emerged as a significant global concern, necessitating the urgent development of new antibacterial drugs. Antimicrobial peptides (AMPs) are naturally occurring peptides found in various organisms. Coupled with a wide range of antibacterial activity, AMPs are less likely to develop drug resistance and can act as potential agents for treating bacterial infections. However, their characteristics, such as low activity, instability, and toxicity, hinder their clinical application. Consequently, researchers are inclined towards artificial design and optimization based on natural AMPs. This review discusses the research advancements in the field of artificial designing and optimization of various AMPs. Moreover, it highlights various strategies for designing such peptides, aiming to provide valuable insights for developing novel AMPs.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1002/bit.28886 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Characterization of S-glycosylated glycocins containing three disulfides.
J Ind Microbiol Biotechnol
September 2025
Department of Biochemistry University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Glycocins are a growing family of ribosomally synthesized and posttranslationally modified peptides (RiPPs) that are O- and/or S-glycosylated. Using a sequence similarity network of putative glycosyltransferases, the thg biosynthetic gene cluster was identified in the genome of Thermoanaerobacterium thermosaccharolyticum. Heterologous expression in Escherichia coli showed that the glycosyltransferase (ThgS) encoded in the biosynthetic gene cluster (BGC) adds N-acetyl-glucosamine (GlcNAc) to Ser and Cys residues of ThgA.
View Article and Find Full Text PDFCan antimicrobial peptides provide an improved antimicrobial strategy for treatment of prosthetic joint infection?
Microbiol Spectr
September 2025
USDA, Agricultural Research Service, Southern Regional Research Center, New Orleans, Louisiana, USA.
With increasing antibiotic resistance and the paucity of new antibiotics in the development pipeline, exploration of antimicrobial peptide applications alone or in combination with existing antibiotics is more crucial than ever. The recent study by J. Varin-Simon, E.
View Article and Find Full Text PDFSynergistic antimicrobial and antibiofilm effects of plant-active ingredients and antibiotics on multidrug-resistant Acinetobacter baumannii.
J Appl Microbiol
September 2025
Sivas Cumhuriyet University, Faculty of Medicine, Department of Medical Microbiology, 58140 Sivas, Türkiye.
Aims: The increasing antimicrobial resistance, particularly in Acinetobacter baumannii, complicates the treatment of infections, leading to higher morbidity, mortality, and economic costs. Herein, we aimed to determine the in vitro antimicrobial, synergistic, and antibiofilm activities of colistin (COL), meropenem, and ciprofloxacin antibiotics, and curcumin, punicalagin, geraniol (GER), and linalool (LIN) plant-active ingredients alone and in combination against 31 multidrug-resistant (MDR) A. baumannii clinical isolates.
View Article and Find Full Text PDFLL-37 and Its Truncated Fragments Modulate Amyloid-β Dynamics, Aggregation and Toxicity Through Hetero-Oligomer and Cluster Formation.
Angew Chem Int Ed Engl
September 2025
Department of Biology and Chemistry, Paul Scherrer Institute, Forschungsstrasse 111, Villigen, PSI, 5232, Switzerland.
LL-37 and its variants with amphiphilic structure can modulate amyloid-β (Aβ) fibril formation, but the detailed mechanism behind it is still unclear. By using four different peptides (LL-37, LL-37, LL-37, LL-37), we found these peptides affect Aβ40 aggregation differently. Nanoscale analysis showed that all LL-37 peptides form hetero-oligomers and nanoclusters with Aβ40, but LL-37 and LL-37, which exhibit the strongest inhibition of Aβ fibrillation, form more hetero-oligomers and smaller nanoclusters.
View Article and Find Full Text PDFFrom the sting to the laboratory: A review of the venom peptides of social wasps (Hymenoptera: Vespidae).
Toxicon
September 2025
Instituto Nacional de Pesquisas da Amazônia - INPA.
Social wasps make up a significant part to the diversity of the Hymenoptera order, one of the most varied insect groups. Beyond their ecological importance, these insects use their venom for defense, protecting their colonies. The venom of social wasps are rich in biologically active substances, including biogenic amines, peptides, proteins, enzymes, allergens, and volatile compounds.
View Article and Find Full Text PDF