Reversible and noncompetitive inhibition of β-tryptase by protein surface binding of tetravalent peptide ligands identified from a combinatorial split-mix library

Abstract

(Figure Presented) Molecular plug: On-bead screening of a combinatorial library of 216 tetravalent oligopeptides reveals highly specific, noncompetitive inhibitors of the serine protease β-tryptase with nanomolar affinity. The ligands most likely bind to the protein surface and act as a molecular plug that blocks access to the active sites, which are buried inside a central cavity (see picture). © 2010 Wiley-VCH Verlag GmbH & Co. KGaA.