The design and synthesis of inhibitors of the cysteinyl protease, Der p I

Bioorg Med Chem Lett. 1998 May 5;8(9):993-8. doi: 10.1016/s0960-894x(98)00151-6.

Abstract

Prototype irreversible inhibitors of the cysteinyl protease Der p I were designed, synthesised and evaluated in vitro. Candidates were designed using a modular approach, whereby a peptide sequence was appended with known thiophilic moieties. This hinged on utilizing peptide sequences from substrate specificity data compiled using proprietary RAPiD technology.

MeSH terms

  • Animals
  • Antigens, Dermatophagoides
  • B-Lymphocytes
  • Cell Line
  • Cysteine Endopeptidases / metabolism*
  • Cysteine Proteinase Inhibitors / chemical synthesis*
  • Cysteine Proteinase Inhibitors / chemistry
  • Cysteine Proteinase Inhibitors / pharmacology
  • Drug Design
  • Feces
  • Glycoproteins / antagonists & inhibitors*
  • Glycoproteins / isolation & purification
  • Humans
  • Mites / enzymology
  • Mites / immunology
  • Molecular Structure
  • Structure-Activity Relationship
  • Substrate Specificity
  • Sulfones / chemical synthesis*
  • Sulfones / chemistry
  • Sulfones / pharmacology
  • Vinyl Compounds / chemical synthesis
  • Vinyl Compounds / chemistry
  • Vinyl Compounds / pharmacology

Substances

  • Antigens, Dermatophagoides
  • Cysteine Proteinase Inhibitors
  • Glycoproteins
  • Sulfones
  • Vinyl Compounds
  • Cysteine Endopeptidases