The design of potent, selective, non-covalent, peptide thrombin inhibitors utilizing imidazole as a S1 binding element

Bioorg Med Chem Lett. 1999 Sep 20;9(18):2767-72. doi: 10.1016/s0960-894x(99)00459-x.

Abstract

Modeling of neutral or mildly basic functional groups in the S1 site of thrombin led to the targeting of imidazole as a S1 binding element and correctly predicted the optimal chain length for connecting this group with the S2 and S3 binding elements. Derivatives of 4-(3-aminopropyl)-imidazole can be selective inhibitors of thrombin demonstrating potent anticoagulant activity.

MeSH terms

  • Antithrombins / chemical synthesis*
  • Antithrombins / chemistry
  • Antithrombins / pharmacology
  • Binding Sites
  • Crystallography, X-Ray
  • Drug Design
  • Humans
  • Imidazoles / metabolism*
  • Models, Molecular
  • Peptides / chemical synthesis*
  • Peptides / chemistry
  • Peptides / pharmacology

Substances

  • Antithrombins
  • Imidazoles
  • Peptides