ArticleAntibiotics (Basel, Switzerland)2023
Modified CLEC3A-Derived Antimicrobial Peptides Lead to Enhanced Antimicrobial Activity against Drug-Resistant Bacteria.
Article in Antibiotics (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Integrative computational-experimental discovery and translation of antifungal peptides for multidrug-resistant fungi.Frontiers in microbiology · 2026Review
- CLEC3A-derived peptides exhibit broad-spectrum activity againstFrontiers in cellular and infection microbiology · 2026Article
- Integrating a cationic backbone with a hydrophobic core: A structure-function strategy for designing self-assembling antimicrobial peptides with enhanced activity.Zoological research · 2025Article
- Antimicrobial peptides: from discovery to developmental applications.Applied and environmental microbiology · 2025Review
- Antimicrobial peptide biological activity, delivery systems and clinical translation status and challenges.Journal of translational medicine · 2025Review
- CLEC3A-Derived Antimicrobial Peptides ReducePharmaceutics · 2025Article
- Diversity and Mechanisms of Action of Plant, Animal, and Human Antimicrobial Peptides.Antibiotics (Basel, Switzerland) · 2024Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Antimicrobial peptides (AMPs) represent a promising alternative to conventional antibiotics. Sequence changes can significantly improve the therapeutic properties of antimicrobial peptides. In our study, we apply different sequence modifications to enhance the performance of the CLEC3A-derived AMPs HT-16 and HT-47. We truncated their sequences, inserting a triple-glycine linker, adding an N-terminal tryptophan residue, and generating a D-amino acid variant, resulting in the generation of seven new peptides. We investigated their antimicrobial activity against gram-positive and gram-negative bacteria, their cytotoxicity to murine cells, and the biostability of the modified peptides in serum. We identified a novel antimicrobial peptide, WRK-30, with enhanced antimicrobial potency against
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.