SALT LAKE CITY, October 14, 2025 — A University of Utah team has shown that a radical enzyme can "tie off" therapeutic peptides into compact rings without the usual leader-sequence requirements, an advance now moving from campus to clinic-facing development through Utah spinout Sethera Therapeutics. The findings have been published in a paper in the prestigious ACS Bio & Med Chem Au Journal.
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Key Takeaways:
- PapB enzyme enables peptide macrocyclization without traditional leader sequences, allowing researchers to modify therapeutic peptides across multiple scaffolds with minimal re-engineering required.
- C-terminal ring formation blocks proteases and stabilizes receptor binding, directly addressing stability and tissue-targeting challenges in next-generation GLP-1 therapies for patients.
- The University of Utah's enzymatic platform is moving toward commercialization through Sethera Therapeutics, shortening the bench-to-bedside pathway for incretin medicines with capital-efficient development.
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About Sethera Therapeutics
For more information about partnering with Sethera, please visit https://setheratx.com/.
Contacts:
Chelli Miller
219-921-6823
[email protected]
Source: Sethera Therapeutics
Distributed by: Reportable, Inc.













