ArticleJournal of the American Chemical Society2017
Lasso Peptide Benenodin-1 Is a Thermally Actuated [1]Rotaxane Switch.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026Review
- Lasso Peptide Syanodin I: Loop-Pulling Two-Step Thermal Unthreading Mechanism.Analytical chemistry · 2025Article
- Expanding the Chemical Space of Mechanically Interlocked Peptides (MIPs) via Rational Design and Metabolite Profiling.JACS Au · 2025Article
- AlphaLasso-a web server to identify loop and lasso motifs in 3D structure of biopolymers.Nucleic acids research · 2025Article
- LassoPred: a tool to predict the 3D structure of lasso peptides.Nature communications · 2025Article
- The potential of bacteriocins and bacteriophages to control bacterial disease of crops with a focus onJournal of the Royal Society of New Zealand · 2025Review
- Advances in lasso peptide discovery, biosynthesis, and function.Trends in genetics : TIG · 2024Review
- Controlled interconversion of macrocyclic atropisomers via defined intermediates.Nature communications · 2024Article
- Article
- Utilization of lasso peptides for biodegradation of polycyclic aromatic hydrocarbons.Environmental microbiology reports · 2024Article
- Discovery, Characterization, and Bioactivity of the Achromonodins: Lasso Peptides Encoded byJournal of natural products · 2023Article
- Mutexa: A Computational Ecosystem for Intelligent Protein Engineering.Journal of chemical theory and computation · 2023Review
- LassoHTP: A High-Throughput Computational Tool for Lasso Peptide Structure Construction and Modeling.Journal of chemical information and modeling · 2023Article
- Peptide/protein-based macrocycles: from biological synthesis to biomedical applications.RSC chemical biology · 2022Review
- Unusual Post-Translational Modifications in the Biosynthesis of Lasso Peptides.International journal of molecular sciences · 2022Review
- Programmable protein topology via SpyCatcher-SpyTag chemistry in one-pot cell-free expression system.Protein science : a publication of the Protein Society · 2022Article
- The Shuttling Cascade in Lasso Peptide Benenodin-1 is Controlled by Non-Covalent Interactions.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Bioinformatics-Guided Expansion and Discovery of Graspetides.ACS chemical biology · 2021Article
- A Bifunctional Leader Peptidase/ABC Transporter Protein Is Involved in the Maturation of the Lasso Peptide Cochonodin I fromJournal of natural products · 2021Article
- Rational generation of lasso peptides based on biosynthetic gene mutations and site-selective chemical modifications.Chemical science · 2021Article
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4 authors.
Funding
Abstract
Mechanically interlocked molecules that change their conformation in response to stimuli have been developed by synthetic chemists as building blocks for molecular machines. Here we describe a natural product, the lasso peptide benenodin-1, which exhibits conformational switching between two distinct threaded conformers upon actuation by heat. We have determined the structures of both conformers and have characterized the kinetics and energetics of the conformational switch. Single amino acid substitutions to benenodin-1 generate peptides that are biased to a single conformer, showing that the switching behavior is potentially an evolvable trait in these peptides. Lasso peptides such as benenodin-1 can be recognized and cleaved by enzymes called lasso peptide isopeptidases. We show that only the native conformer of benenodin-1 is cleaved by its cognate isopeptidase. Thus, thermally induced conformational switching of benenodin-1 may also be relevant to the biological function of these molecules.
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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.