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Lasso Peptide Syanodin I: Loop-Pulling Two-Step Thermal Unthreading Mechanism.

Miguel Santos-Fernandez1, Kevin Jeanne Dit Fouque1,2, Ukesh Karki3

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Analytical Chemistry
|October 28, 2025
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The thermal unfolding of lasso peptides, like syanodin I, involves a two-step mechanism. This process is driven by steric constraints and involves loop-pulling of the peptide tail, as revealed by advanced mass spectrometry and simulations.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Chemical Physics

Background:

  • Lasso peptides are ribosomally synthesized and post-translationally modified peptides (RiPPs).
  • They feature a C-terminal tail threaded through an N-terminal macrolactam ring, forming a unique topology.
  • Understanding their structural dynamics, especially thermal stability, is crucial for their function.

Purpose of the Study:

  • To characterize the thermal unthreading process of the lasso peptide syanodin I.
  • To identify kinetic intermediates and elucidate the unfolding mechanism.
  • To investigate the role of specific residues in maintaining the lasso structure.

Main Methods:

  • Liquid chromatography-trapped ion mobility spectrometry-electron-capture dissociation-tandem mass spectrometry (LC-TIMS-q-ECD-ToF MS/MS).
  • Steered molecular dynamics (SMD) simulations.
  • Site-directed mutagenesis studies.

Main Results:

  • Identified kinetic intermediates of syanodin I during thermal unfolding using LC-TIMS-q-ECD-ToF MS/MS.
  • Mutagenesis confirmed Leu15 as a key residue in an intermediate lasso structure.
  • Observed a two-step thermal unfolding mechanism involving loop-pulling and potentially tail-pulling, supported by SMD simulations.

Conclusions:

  • Syanodin I exhibits a two-step thermal unfolding mechanism driven by steric constraints.
  • The process involves loop-pulling of the lasso tail, with potential contributions from tail-pulling.
  • This study provides the first report of such a mechanism in lasso peptides.