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Protein engineering can create Pierced Lasso (PL) topologies by introducing disulfide bridges. Loop size dictates threading mechanisms, impacting protein dynamics and biological activity crucial for receptor interaction.

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Area of Science:

  • Protein Engineering
  • Structural Biology
  • Biophysics

Background:

  • Disulfide bridges stabilize proteins in drug design but can form covalent loops.
  • These loops can lead to complex topologies like Pierced Lassos (PL), where a polypeptide chain is threaded through a loop.

Purpose of the Study:

  • To investigate the threading mechanisms of Pierced Lasso topologies.
  • To understand how loop size and position influence protein dynamics and biological activity.

Main Methods:

  • Designed three loop variants of a Pierced Lasso protein to mimic natural polymorphic sequences.
  • Studied the effect of loop size on threading mechanisms (slipknotting vs. plugging).
  • Assessed the impact of topology on protein dynamics and biological activity.

Main Results:

  • Loop size was shown to alter the threading mechanism from slipknotting to plugging.
  • Protein ground state structure remained largely unaffected by loop modifications.
  • Biological assays revealed maximized activity in the threaded state due to controlled dynamics.

Conclusions:

  • Pierced Lasso topology and conformational dynamics are critical for receptor interaction and signaling.
  • Protein engineering offers a way to manipulate these topologies for therapeutic applications.
  • Understanding threading mechanisms provides insights into protein folding and function.