Substituted Isatoic Anhydrides: Selective Inactivators of Trypsin-like Serine Proteases

Article abstract of DOI:10.1021/jm00154a026

Derivatives of isatoic anhydride were prepared and tested as inhibitors of serine proteases.A number of isatoic anhydrides with positively charged substituents irreversibly inactivated several trypsin-like enzymes and preferentially inactivated trypsin over chymotrypsin.Further selectivity was obtained by introduction of an aromatic group on the N-1 position of isatoic anhydride. 7-(Aminomethyl)-1-benzylisatoic anhydride was prepared and was a selective inactivator of thrombin; thus it is possible to prepare derivatives of isatoic anhydride that are highly enzyme selective without attaching peptide recognition structures.