Valaminols, probably the most simplified peptide-analogs acting as pepsin inhibitors.
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.
Kratzel
M
M
Institute of Pharmaceutical Chemistry, University of Vienna, Althanstrasse 14, A-1090, Vienna, Austria. kratzel@speedy.pch.univie.ac.at
Bernkop-Schnürch
A
A
D015195:Drug Design; D006735:Horseradish Peroxidase; D015394:Molecular Structure; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000494:pharmacology; D010434:Pepsin A / Q000037:antagonists & inhibitors*; D010436:Pepstatins / Q000737:chemistry / Q000494:pharmacology; D010455:Peptides / Q000737:chemistry* / Q000494:pharmacology; D011480:Protease Inhibitors / Q000138:chemical synthesis*; D013329:Structure-Activity Relationship
D009842:Oligopeptides; D010436:Pepstatins; D010455:Peptides; D011480:Protease Inhibitors; C014195:Streptomyces pepsin inhibitor; D006735:Horseradish Peroxidase; D010434:Pepsin A; C031375:pepstatin