Unraveling sub-site specificities of peptidic serine protease inhibitors by substitutional and structural analysis.
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.
Höhne
Wolfgang
W
Charité - Universitätsmedizin Berlin, Institut für Biochemie, Monbijoustr.2a, D-10117 Berlin. wolfgang.hochme@charite.de
Hilpert
Kai
K
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
D015842:Serine Proteinase Inhibitors; D012697:Serine Endopeptidases