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Showing 1–3 of 3 results

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The proline-rich antimicrobial peptide Api137 disrupts large ribosomal subunit assembly and induces misfolding

Proline-rich antimicrobial peptides (PrAMPs) are inhibitors of bacterial protein synthesis. Here, the authors demonstrate that the antimicrobial peptide Api137 can disrupt assembly of the ribosomal 50S subunit by inducing misfolding of its components.

Simon Malte Lauer
Jakob Gasse
Ralf Hoffmann
ResearchOpen Access10 Jan 2025
Nature Communications

Volume: 16, P: 1-18
Inhibition of translation termination by the antimicrobial peptide Drosocin

The antimicrobial peptide Drosocin encoded in the fruit fly genome inhibits bacterial translation by stalling the ribosomes at stop codons, sequestering class 1 release factors and inducing stop codon readthrough. Comprehensive mutational analysis reveals key activity determinants of Drosocin.

Kyle Mangano
Dorota Klepacki
Alexander S. Mankin
Research30 Mar 2023
Nature Chemical Biology

Volume: 19, P: 1082-1090
Multimodal binding and inhibition of bacterial ribosomes by the antimicrobial peptides Api137 and Api88

Proline-rich antimicrobial peptides (PrAMPs) inhibit bacterial protein biosynthesis. Here, the authors show that the honey-bee derived PrAMPs Api137 and Api88 inhibit bacterial ribosomes through multiple mechanisms, promising for drug development.

Simon M. Lauer
Maren Reepmeyer
Ralf Hoffmann
ResearchOpen Access10 May 2024
Nature Communications

Volume: 15, P: 1-19