INTERACTION OF A PEPTIDOMIMETIC AMINIMIDE INHIBITOR WITH ELASTASE

The crystal structure of an aminimide analog of a dipeptide inhibitor of porcine pancreatic elastase bound to its target serine protease has been solved. The peptidomimetic molecule binds in the same fashion as the class of dipeptides from which it was derived, making similar int eractions with the subsites on the elastase surface. Because aminimide s are readily synthesized from a wide variety of starting materials, t hey form the basis for a combinatorial chemistry approach to rational drug design.