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New Cyanopeptide‐Derived Low Molecular Weight Inhibitors of trypsin‐like Serine Proteases
Author(s) -
Radau Gregor,
Schermuly Sonja,
Fritsche Alexandra
Publication year - 2003
Publication title -
archiv der pharmazie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 61
eISSN - 1521-4184
pISSN - 0365-6233
DOI - 10.1002/ardp.200300765
Subject(s) - proteases , serine , chemistry , trypsin , thrombin , biochemistry , serine proteinase inhibitors , enzyme , biological activity , serine protease , lead compound , enzyme inhibitor , stereochemistry , protease , biology , in vitro , platelet , immunology
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.