Structure-activity and crystallographic analysis of a new class of non-amide-based thrombin inhibitor

Bioorg Med Chem Lett. 2000 Jan 3;10(1):79-82. doi: 10.1016/s0960-894x(99)00617-4.

Abstract

The structure activity relationships of a novel series of non-amide-based thrombin inhibitors are described. Exploration of the P2 and the aryl binding region for this series has identified optimal groups for achieving nanomolar potency. The binding modes of these optimal groups have been confirmed by X-ray structural analysis.

MeSH terms

  • Amides / chemistry
  • Antithrombins / chemistry*
  • Antithrombins / pharmacology*
  • Arylsulfonates / chemistry
  • Arylsulfonates / pharmacology
  • Binding Sites
  • Crystallography, X-Ray
  • Models, Molecular
  • Piperidines / chemistry*
  • Piperidines / pharmacology*
  • Serine Proteinase Inhibitors / chemistry
  • Serine Proteinase Inhibitors / classification
  • Serine Proteinase Inhibitors / pharmacology
  • Structure-Activity Relationship
  • Thrombin / antagonists & inhibitors*

Substances

  • Amides
  • Antithrombins
  • Arylsulfonates
  • Piperidines
  • Serine Proteinase Inhibitors
  • Thrombin