title: Unraveling sub-site specificities of peptidic serine protease inhibitors by substitutional and structural analysis.
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.
authors: Charité - Universitätsmedizin Berlin, Institut für Biochemie, Monbijoustr.2a, D-10117 Berlin. wolfgang.hochme@charite.de
authors: Wolfgang
authors: W
authors: Höhne
authors: Kai
authors: K
authors: Hilpert
mesh_terms: D019943:Amino Acid Substitution; D018360:Crystallography, X-Ray; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012697:Serine Endopeptidases / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000502:physiology*; D013329:Structure-Activity Relationship
chemical_list: D015842:Serine Proteinase Inhibitors; D012697:Serine Endopeptidases