ArticleInternational journal of molecular sciences2021
Generation of Lasso Peptide-Based ClpP Binders.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026Review
- Merging Flow Synthesis and Enzymatic Maturation to Expand the Chemical Space of Lasso Peptides.Journal of the American Chemical Society · 2024Article
- Identification of macrocyclic peptides which activate bacterial cylindrical proteases.RSC medicinal chemistry · 2023Article
- Therapeutic Targeting of the Proteolytic Enzymes.International journal of molecular sciences · 2022Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The Clp protease system fulfills a plethora of important functions in bacteria. It consists of a tetradecameric ClpP barrel holding the proteolytic centers and two hexameric Clp-ATPase rings, which recognize, unfold, and then feed substrate proteins into the ClpP barrel for proteolytic degradation. Flexible loops carrying conserved tripeptide motifs protrude from the Clp-ATPases and bind into hydrophobic pockets (H-pockets) on ClpP. Here, we set out to engineer microcin J25 (MccJ25), a ribosomally synthesized and post-translationally modified peptide (RiPP) of the lasso peptide subfamily, by introducing the conserved tripeptide motifs into the lasso peptide loop region to mimic the Clp-ATPase loops. We studied the capacity of the resulting lasso peptide variants to bind to ClpP and affect its activity. From the nine variants generated, one in particular (12IGF) was able to activate ClpP from
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