Science Advances, Год журнала: 2025, Номер 11(21)

Опубликована: Май 21, 2025

Site-selective chemical peptide manipulation is an effective strategy to understand and regulate structure function. However, methionine-selective modification remains one of the most difficult challenges in chemistry, with notable limited strategies. In this study, we report a general reversible at methionine sites that uses ruthenium-catalyzed sulfimidation peptides. This method provides convenient for late-stage functionalization. The N═S bonds conjugates are reduced presence glutathione, resulting traceless releasing corresponding peptides amides. Practical applications then demonstrated using precise modifications bioactive peptides, stapling linearization peptide-drug conjugates, split-and-pool synthesis. on/off through unique tool chemistry peptide-based drug discovery.

Язык: Английский