title: D-Phe-Pro-Arg type thrombin inhibitors: unexpected selectivity by modification of the P1 moiety.
abstract: Synthesis of thrombin inhibitors and their binding mode to thrombin is described. Modification of the P1 moiety leads to an increased selectivity versus trypsin. The observed selectivity is discussed in view of their thrombin-inhibitor complex X-ray structures.
authors.affiliation: BASF AG, D-67056, Ludwigshafen, Germany. wolfgang.hoeffken@basf-ag.de
authors.forename: Udo E W
authors.initials: UE
authors.lastname: Lange
authors.forename: Dorit
authors.initials: D
authors.lastname: Baucke
authors.forename: Wilfried
authors.initials: W
authors.lastname: Hornberger
authors.forename: Helmut
authors.initials: H
authors.lastname: Mack
authors.forename: Werner
authors.initials: W
authors.lastname: Seitz
authors.forename: H Wolfgang
authors.initials: HW
authors.lastname: Höffken
mesh_terms: D018360:Crystallography, X-Ray; D015195:Drug Design; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry* / Q000494:pharmacology*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013917:Thrombin / Q000037:antagonists & inhibitors* / Q000378:metabolism; D014361:Trypsin Inhibitors / Q000737:chemistry / Q000494:pharmacology
chemical_list: D004791:Enzyme Inhibitors; D009842:Oligopeptides; D014361:Trypsin Inhibitors; C077952:phenylalanyl-prolyl-arginine; D013917:Thrombin