New cyanopeptide-derived low molecular weight inhibitors of trypsin-like serine proteases.
This paper deals with the design, syntheses, and inhibition tests of new low molecular weight thrombin inhibitors utilizing cyanopeptides, the secondary metabolites of cyanobacteria with interesting biological activities, as new lead structures. Starting with aeruginosin 98-B (1) as a lead structure, we have developed and synthesised new, selective acting inhibitors of serine proteases (RA-1005 and RA-1009, which are suitable targets for further structure-activity studies.
Radau
Gregor
G
Institute of Pharmacy, Ernst-Moritz-Arndt-University Greifswald, Pharmaceutical/Medicinal Chemistry, Greifswald, Germany. radau@pharmazie.uni-greifswald.de
Schermuly
Sonja
S
Fritsche
Alexandra
A
D000458:Cyanobacteria / Q000737:chemistry; D015195:Drug Design; D008970:Molecular Weight; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry; D012697:Serine Endopeptidases / Q000737:chemistry*; D015842:Serine Proteinase Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry; D013329:Structure-Activity Relationship
D009842:Oligopeptides; D015842:Serine Proteinase Inhibitors; C472547:aeruginosin 98-B; C114880:trypsin-like serine protease; D012697:Serine Endopeptidases