SALT LAKE CITY, Utah August 21, 2025 — Sethera Therapeutics today announced publication in the Proceedings of the National Academy of Sciences (PNAS) of peer-reviewed results describing an enzymatic crosslinking platform that forges durable thioether “staples,” locking peptides into drug-like cyclic architectures. The platform works across a broad range of substrates, including sequences built entirely from non-natural building blocks, delivering exceptional versatility, expanding accessible chemical space, and enabling the design of next-generation peptide therapeutics.
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Key Takeaways:
- Radical-Based Enzymatic Technology: Sethera's breakthrough platform acts like a precise "molecular stapler," creating durable thioether "staples" that are chemically robust and protease-resistant - superior to traditional disulfide bonds found in natural peptides.
- Controlled "Promiscuity" with Precision: The platform shows broad substrate scope, accepting non-natural building blocks (D-amino acids, β-amino acids, N-methyl residues) while directing exactly where bonds form - expanding accessible chemical space for next-generation therapeutics.
- PNAS Publication Validates Impact: Peer-reviewed results in Proceedings of the National Academy of Sciences demonstrate the technology's potential to lead the next wave of innovation in peptide therapeutics, directly connecting to GLP-1s, insulins, and natural hormone design.
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About Sethera Therapeutics
Sethera Therapeutics is developing internal programs and collaborations that leverage its enzymatic macrocyclization platform to create more effective, stable, and deliverable peptide medicines. By opening vast new design space and offering precise architectural control, Sethera is positioned to help lead the next wave of innovation in peptide therapeutics.
Contacts:
Karsten Eastman, PhD, CEO
385-461-8528
[email protected]
Source: Sethera Therapeutics
Distributed by: Reportable, Inc.
