ArticleNature chemical biology2023
An anti-biofilm cyclic peptide targets a secreted aminopeptidase from P. aeruginosa.
Article in Nature chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 24 citations in OpenAlex.
- Biosynthesis of Silver Nanoparticles fromBiology · 2026Article
- Biotechnological Potential of Algerian Saffron Floral Residues: Recycling Phytochemicals with Antimicrobial Activity.Biology · 2026Article
- Extracellular aminopeptidase regulates exopolysaccharide production of Pseudomonas aeruginosa via quorum sensing.The ISME journal · 2025Article
- Framework nucleic acid strategy enables closer microbial contact for programming short-range interaction.Science advances · 2024Article
- cyclicpeptide: a Python package for cyclic peptide drug design.Briefings in bioinformatics · 2024Article
- Structural determinants of protein kinase A essential for CFTR channel activation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- New 24-Membered Macrolactines from an Arctic BacteriumMarine drugs · 2024Article
- The Secreted Aminopeptidase ofInternational journal of molecular sciences · 2024Review
- Exploring roles of the chitinase ChiC in modulatingMicrobiology spectrum · 2024Article
- Exoproteome analysis of Pseudomonas aeruginosa response to high alkane stress.Archives of microbiology · 2024Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Pseudomonas aeruginosa is an opportunistic pathogen that causes serious illness, especially in immunocompromised individuals. P. aeruginosa forms biofilms that contribute to growth and persistence in a wide range of environments. Here we investigated the aminopeptidase, P. aeruginosa aminopeptidase (PaAP) from P. aeruginosa, which is highly abundant in the biofilm matrix. PaAP is associated with biofilm development and contributes to nutrient recycling. We confirmed that post-translational processing was required for activation and PaAP is a promiscuous aminopeptidase acting on unstructured regions of peptides and proteins. Crystal structures of wild-type enzymes and variants revealed the mechanism of autoinhibition, whereby the C-terminal propeptide locks the protease-associated domain and the catalytic peptidase domain into a self-inhibited conformation. Inspired by this, we designed a highly potent small cyclic-peptide inhibitor that recapitulates the deleterious phenotype observed with a PaAP deletion variant in biofilm assays and present a path toward targeting secreted proteins in a biofilm context.
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Registered trials
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