Abstract
The interaction of peptidic inhibitors with serine proteases is investigated using peptide spot synthesis on cellulose sheets. This method permits a highly parallel analysis of subsite specificities and an optimization of peptidic inhibitors towards higher affinity and specificity for a given target protease. Information from crystal structures of corresponding protease/inhibitor complexes may help to explain the observed binding pattern.
Keywords: serine protease, elastase, peptidic inhibitor, ovomucoid inhibitor, peptide spot synthesis, substitutional analysis, subsite specificity, x-ray structure