Abstract
The formation of structurally defined bioconjugates of proteins hinges on their regioselective modification. Toward this goal a novel method is described here using the commercial IgA protease to attach a nonnatural peptidic moiety to the N-terminus of predisposed proteins by means of a kinetically controlled reverse proteolysis in water. The process requires an H-Ala-Pro N-terminal sequence and then furnishes a selectively modified conjugate under nondenaturing and nondestructive conditions in acceptable yield. The method lends itself to the N-terminal introduction of orthogonal moieties that may be elaborated further.
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