Biocatalytic shortcut gives GLP-1-like peptides a makeover, boosting stability and potential for new therapies

GLP-1–pathway agonists such as semaglutide and newer multi-agonists have transformed care for obesity and diabetes, yet developers still wrestle with durability, tissue targeting, and signal “bias.” Macrocyclization, tying part of a peptide into a ring, can shield drugs from degradation and favor bioactive shapes, but conventional chemistry can be costly and hard to apply late in development.

A research team at Sethera Therapeutics and the Bandarian Lab at the University of Utah has shown that a radical enzyme can “tie off” therapeutic peptides into compact rings without the usual leader-sequence requirements.

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