Significance Influenza remains a major global health threat . We introduce oseltamivir-based aziridines that unite transition-state mimicry for tight binding with aziridine-enabled covalent capture of the catalytic tyrosine . This dual function yields potent, mechanism-based neuraminidase inhibition and enables activity-based quantification of active enzyme directly in complex samples. Across N1, N2, and influenza B enzymes , selected compounds show high potency against diverse viral neuraminidases and in live virus replication assays. By combining a clinically grounded scaffold with a reactivity handle, these molecules bridge therapeutic and diagnostic needs and offer a practical platform for neuraminidase imaging and antiviral development. Abstract Influenza neuraminidase (NA) is a critical target for seasonal and pandemic antivirals , including the strains of current concern. Current treatments, such as Zanamivir and Oseltamivir , are limited by noncovalent binding and emergin...
Media Monitoring for Signals about Emerging Threats