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Cystine Knot Peptides with Tuneable Activity and Mechanism.

Choi Yi Li1, Fabian B H Rehm1, Kuok Yap1

  • 1Institute for Molecular Bioscience, Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, The University of Queensland, Brisbane, QLD 4072, Australia.

Angewandte Chemie (International Ed. in English)
|February 28, 2022
PubMed
Summary

Engineered knottins offer new ways to control protease inhibitors using light or streptavidin. This allows precise ON/OFF switching of inhibitor activity for diverse biological applications.

Keywords:
Activity SwitchEnzymesInhibitorsKnottinsPhotoactivation

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Knottins are structurally complex peptides stabilized by a cystine knot, exhibiting diverse biological functions like protease inhibition.
  • Current methods for modulating knottin activity in situ are limited, hindering their therapeutic and research applications.

Purpose of the Study:

  • To develop novel strategies for dynamically controlling the activity and selectivity of knottin protease inhibitors.
  • To engineer knottins for light-inducible activation and streptavidin-mediated inactivation.

Main Methods:

  • Utilized a knottin library screen to identify optimal sites for functional modifications.
  • Engineered a knottin protease inhibitor for light-activated secondary mode of action.
  • Developed a biotinylated knottin variant for streptavidin-dependent activity modulation.

Main Results:

  • Demonstrated light-induced switching of knottin inhibitory activity and target selectivity.
  • Identified a specific binding loop position for biotinylation without compromising knottin activity.
  • Showcased rapid inactivation of biotinylated knottins and a factor XIIa inhibitor in plasma using streptavidin.

Conclusions:

  • Developed versatile light and streptavidin-based systems for precise control over knottin protease inhibitor function.
  • Expanded the toolkit for engineering knottins with tunable activity for advanced biological research and potential therapeutics.