Binding structure of elastase inhibitor scyptolin A.

Natural bioactive compounds are of general interest to pharmaceutical research because they may be used as leads in drug development campaigns. Among them, scyptolin A and B from Scytonema hofmanni PCC 7110 are known to inhibit porcine pancreatic elastase, which in turn resembles the attractive drug target neutrophil elastase. The crystal structure of scyptolin A as bound to pancreatic elastase was solved at 2.

Hofmannolin, a cyanopeptolin from Scytonema hofmanni PCC 7110.

Two depsipeptide metabolites, scyptolin A and B, were reported recently from the axenically grown terrestrial cyanobacterium Scytonema hofmanni PCC 7110. A related, novel depsipeptide was isolated from this Scytonema and designated hofmannolin. The amino acid analysis in context with infrared, mass and 1H/13C-NMR spectroscopies revealed a cyclic depsipeptide structure of M(r) 1073 belonging to the class of cyanopeptolins.