Design of Small-Molecule Active-Site Inhibitors of the S1A Family Proteases as Procoagulant and Anticoagulant Drugs

J Med Chem. 2018 May 10;61(9):3799-3822. doi: 10.1021/acs.jmedchem.7b00772. Epub 2017 Nov 9.

Abstract

Vitamin K antagonists (VKA) have long been the default drugs for anticoagulant management in venous thrombosis. While efficacious, they are difficult to use due to interpatient dose-response variability and the risks of bleeding. The approval of fondaparinux, a heparin-derived factor Xa (fXa) inhibitor, provided validation for the development of direct oral anticoagulants (DOAC), and currently such inhibitors of thrombin and fXa are in clinical use. These agents can be used without regular coagulation monitoring, but the inherent risk of bleeding complications associated with blocking the common coagulation pathway remains. Efforts are now underway to develop DOACs that inhibit components of the intrinsic and extrinsic coagulation cascades upstream of thrombin and fX. Evidence from humans and from transgenic animal models suggests that this strategy may provide a better therapeutic margin between antithrombotic and antihemostatic effects. Here the design of active-site inhibitors of S1A proteases involved in coagulation and fibrinolysis is summarized.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anticoagulants / pharmacology*
  • Blood Coagulation / drug effects*
  • Catalytic Domain / drug effects*
  • Humans
  • Peptide Hydrolases / chemistry*
  • Peptide Hydrolases / metabolism*
  • Protease Inhibitors / pharmacology*
  • Small Molecule Libraries / pharmacology*

Substances

  • Anticoagulants
  • Protease Inhibitors
  • Small Molecule Libraries
  • Peptide Hydrolases