ArticleACS chemical biology2019
Pandonodin: A Proteobacterial Lasso Peptide with an Exceptionally Long C-Terminal Tail.
Article in ACS chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026Review
- Repositioning the Leader Peptide in Graspetide Biosynthesis.Journal of the American Chemical Society · 2026Article
- Dual-probe genome mining identifies citrulassin N, a novel citrulline modified lasso peptide fromFrontiers in microbiology · 2026Article
- Lasso Peptides-A New Weapon Against Superbugs.International journal of molecular sciences · 2025Review
- Discovery and Heterologous Expression of Trilenodin, an Antimicrobial Lasso Peptide with a Unique Tri-Isoleucine Motif.Chembiochem : a European journal of chemical biology · 2024Article
- Advances in lasso peptide discovery, biosynthesis, and function.Trends in genetics : TIG · 2024Review
- Influence of PepF peptidase and sporulation on microcin J25 production inMicrobiology spectrum · 2024Article
- Lasso Peptides: Exploring the Folding Landscape of Nature's Smallest Interlocked Motifs.Journal of the American Chemical Society · 2024Article
- Discovery, Characterization, and Bioactivity of the Achromonodins: Lasso Peptides Encoded byJournal of natural products · 2023Article
- Bacterial natural product discovery by heterologous expression.Journal of industrial microbiology & biotechnology · 2023Review
- LassoHTP: A High-Throughput Computational Tool for Lasso Peptide Structure Construction and Modeling.Journal of chemical information and modeling · 2023Article
- Unusual Post-Translational Modifications in the Biosynthesis of Lasso Peptides.International journal of molecular sciences · 2022Review
- Rational generation of lasso peptides based on biosynthetic gene mutations and site-selective chemical modifications.Chemical science · 2021Article
- Cellulonodin-2 and Lihuanodin: Lasso Peptides with an Aspartimide Post-Translational Modification.Journal of the American Chemical Society · 2021Article
- Heterologous production of new lasso peptide koreensin based on genome mining.The Journal of antibiotics · 2021Article
- Recent Advances and Perspectives on Expanding the Chemical Diversity of Lasso Peptides.Frontiers in bioengineering and biotechnology · 2021Review
- Class IV Lasso Peptides Synergistically Induce Proliferation of Cancer Cells and Sensitize Them to Doxorubicin.iScience · 2020Article
- How to harness biosynthetic gene clusters of lasso peptides.Journal of industrial microbiology & biotechnology · 2020Review
- Lasso Peptides: Heterologous Production and Potential Medical Application.Frontiers in bioengineering and biotechnology · 2020Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Lasso peptides are a family of ribosomally synthesized and post-translationally modified peptides (RiPPs) defined by their threaded-ring topology. The N-terminus of the peptide forms an isopeptide bond with an aspartate or glutamate side chain to create a 7-9 amino acid (aa) macrocyclic ring through which the rest of the peptide is threaded. The result is a highly constrained three-dimensional structure. Even though they share a threaded-ring feature, characterized lasso peptides vary greatly in sequence and size, ranging from 14 to 26 aa. Using genome mining, we identified a new lasso peptide gene cluster with a predicted lasso peptide that is 33 aa long. Here we report the heterologous expression of this new peptide, pandonodin, its NMR structure, and its unusual biophysical properties. Pandonodin has a long, proteolytically resistant 18-residue tail of low sequence complexity, which limits its water solubility. Within this tail is a 6 aa disulfide-bonded macrocycle that serves as a steric lock to maintain the lasso structure. This disulfide bond is unusually stable, requiring both heat and high concentrations of reductants for cleavage. Finally, we also show that segments of the C-terminal tail of pandonodin can be replaced with arbitrary sequences, allowing for the construction of pandonodin-protein fusions.
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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.