Valaminols, probably the most simplified peptide-analogs acting as pepsin inhibitors

Peptides. 2000 Feb;21(2):289-93. doi: 10.1016/s0196-9781(99)00196-5.

Abstract

Recently, we have introduced simplified analogs of pepstatin A, representing 'tripeptides' with two valine residues which are C-terminated by an amino alcohol moiety. In the present study, we have deleted one valine unit, yielding simple molecules-called 'valaminols'-which can be prepared in big scale under really low costs. First investigations on structure-activity relationships revealed that the most active compound is a valaminol bearing both natural substituents either at the N-terminus or at the C-terminal side chain. Its inhibitory activity fully corresponds to the activity of tripeptides, hitherto reported by us, although one valine residue has been omitted.

MeSH terms

  • Drug Design
  • Horseradish Peroxidase
  • Molecular Structure
  • Oligopeptides / chemical synthesis*
  • Oligopeptides / pharmacology
  • Pepsin A / antagonists & inhibitors*
  • Pepstatins / chemistry
  • Pepstatins / pharmacology
  • Peptides / chemistry*
  • Peptides / pharmacology
  • Protease Inhibitors / chemical synthesis*
  • Structure-Activity Relationship

Substances

  • Oligopeptides
  • Pepstatins
  • Peptides
  • Protease Inhibitors
  • Streptomyces pepsin inhibitor
  • Horseradish Peroxidase
  • Pepsin A
  • pepstatin