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...

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Bibliographic Details
Published in:Archiv der Pharmazie (Weinheim) 2003-08, Vol.336 (6-7), p.300-309
Main Authors: Radau, Gregor, Schermuly, Sonja, Fritsche, Alexandra
Format: Article
Language:English
Subjects:
Biological and medical sciences
Blood. Blood coagulation. Reticuloendothelial system
Cyanobacteria
Cyanobacteria - chemistry
Cyanopeptides
Drug Design
Medical sciences
Molecular Weight
Oligopeptides - chemical synthesis
Oligopeptides - chemistry
Peptide syntheses
Pharmacology. Drug treatments
Rational drug design
Serine Endopeptidases - chemistry
Serine Proteinase Inhibitors - chemical synthesis
Serine Proteinase Inhibitors - chemistry
Structure-Activity Relationship
Thrombin inhibitors
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Summary: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.
ISSN:0365-6233
1521-4184
DOI:10.1002/ardp.200300765