Potent thrombin inhibitors that probe the S1 subsite: tripeptide transition state analogues based on a heterocycle-activated carbonyl group

J Med Chem. 1996 Aug 2;39(16):3039-43. doi: 10.1021/jm9603274.
No abstract available

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arginine / analogs & derivatives
  • Binding Sites
  • Cattle
  • Crystallography, X-Ray
  • Guanidines / chemical synthesis*
  • Guanidines / chemistry
  • Guanidines / pharmacology
  • Humans
  • Molecular Sequence Data
  • Molecular Structure
  • Oligopeptides / pharmacology
  • Peptides / chemical synthesis*
  • Peptides / chemistry
  • Peptides / pharmacology
  • Pipecolic Acids / pharmacology
  • Protein Binding
  • Serine Proteinase Inhibitors / chemical synthesis
  • Serine Proteinase Inhibitors / chemistry
  • Serine Proteinase Inhibitors / pharmacology
  • Sulfonamides
  • Thiazoles / chemical synthesis*
  • Thiazoles / chemistry
  • Thiazoles / pharmacology
  • Thrombin / antagonists & inhibitors*
  • Thrombin / chemistry
  • Trypsin Inhibitors / chemical synthesis
  • Trypsin Inhibitors / chemistry
  • Trypsin Inhibitors / pharmacology

Substances

  • Guanidines
  • Oligopeptides
  • Peptides
  • Pipecolic Acids
  • RWJ 50353
  • Serine Proteinase Inhibitors
  • Sulfonamides
  • Thiazoles
  • Trypsin Inhibitors
  • Arginine
  • Thrombin
  • argatroban
  • efegatran