D-Phe-Pro-Arg type thrombin inhibitors: unexpected selectivity by modification of the P1 moiety

Bioorg Med Chem Lett. 2003 Jun 16;13(12):2029-33. doi: 10.1016/s0960-894x(03)00347-0.

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.

MeSH terms

  • Crystallography, X-Ray
  • Drug Design
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / pharmacology*
  • Models, Molecular
  • Oligopeptides / chemistry*
  • Oligopeptides / pharmacology*
  • Structure-Activity Relationship
  • Substrate Specificity
  • Thrombin / antagonists & inhibitors*
  • Thrombin / metabolism
  • Trypsin Inhibitors / chemistry
  • Trypsin Inhibitors / pharmacology

Substances

  • Enzyme Inhibitors
  • Oligopeptides
  • Trypsin Inhibitors
  • phenylalanyl-prolyl-arginine
  • Thrombin