ArticleChembiochem : a European journal of chemical biology2021
Molecular Basis of Selectivity and Activity for the Antimicrobial Peptide Lynronne-1 Informs Rational Design of Peptide with Improved Activity.
Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Antimicrobial Peptides: Mechanism, Expressions, and Optimization Strategies.Probiotics and antimicrobial proteins · 2025Review
- Natural peptides and their synthetic congeners acting againstRSC medicinal chemistry · 2025Review
- Potency of all-D amino acid antimicrobial peptides derived from the bovine rumen microbiome on tuberculous and non-tuberculous mycobacteria.Current research in microbial sciences · 2025Article
- Microbiome-derived antimicrobial peptides show therapeutic activity against the critically important priority pathogen, Acinetobacter baumannii.NPJ biofilms and microbiomes · 2024Article
- Microbial- and Plant-Derived Bioactive Peptides and Their Applications against Foodborne Pathogens: Current Status and Future Prospects.International journal of microbiology · 2024Review
- An Update on the Therapeutic Potential of Antimicrobial Peptides againstPharmaceuticals (Basel, Switzerland) · 2023Review
- Microbiome-derived antimicrobial peptides offer therapeutic solutions for the treatment of Pseudomonas aeruginosa infections.NPJ biofilms and microbiomes · 2022Article
- Molecular Basis of Selectivity and Activity for the Antimicrobial Peptide Lynronne-1 Informs Rational Design of Peptide with Improved Activity.Chembiochem : a European journal of chemical biology · 2021Article
- Antifungal Activity of ToAP2D Peptide AgainstFrontiers in bioengineering and biotechnology · 2021Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Antibiotic resistance is a significant threat to human health, with natural products remaining the best source for new antimicrobial compounds. Antimicrobial peptides (AMPs) are natural products with great potential for clinical use as they are small, amenable to customization, and show broad-spectrum activities. Lynronne-1 is a promising AMP identified in the rumen microbiome that shows broad-spectrum activity against pathogens such as methicillin-resistant Staphylococcus aureus and Acinetobacter baumannii. Here we investigated the structure of Lynronne-1 using solution NMR spectroscopy and identified a 13-residue amphipathic helix containing all six cationic residues. We used biophysical approaches to observe folding, membrane partitioning and membrane lysis selective to the presence of anionic lipids. We translated our understanding of Lynronne-1 structure to design peptides which varied in the size of their hydrophobic helical face. These peptides displayed the predicted continuum of membrane-lysis activities in vitro and in vivo, and yielded a new AMP with 4-fold improved activity against A. baumannii and 32-fold improved activity against S. aureus.
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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.