ArticleAnalytical chemistry2025
Lasso Peptide Syanodin I: Loop-Pulling Two-Step Thermal Unthreading Mechanism.
Article in Analytical chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Biosynthesis, Structure, and Antibiotic Properties of Gelatinamin A, a Triculamin-Like Lasso Peptide.Chembiochem : a European journal of chemical biology · 2026Article
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8 authors.
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Abstract
Lasso peptides are a class of ribosomally synthesized and post-translationally modified peptides (RiPPs) where the C-terminal tail is threaded and sterically trapped within an N-terminal macrolactam ring. In the present work, the thermal unthreading process of the lasso peptide syanodin I was characterized using liquid chromatography, trapped ion mobility spectrometry, electron-capture dissociation, and tandem mass spectrometry (LC-TIMS-q-ECD-ToF MS/MS) and steered molecular dynamics (SMD). The analytical workflow allows for the separation (LC and TIMS) and identification (ECD MS/MS) of syanodin I kinetic intermediates as a function of the solution temperature. The syanodin WT with the plug residue Gln13 can be identified from the branched-cyclic topology based on unique retention time (RT), IMS bands, and hydrogen migration events near the molecular knot (
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