Abstract
Two new potent serine protease inhibitors, cyclotheonamides E2 (3) and E3 (4), have been isolated from a marine sponge of the genus Theonella. Their structures were determined by interpretation of spectral data and chemical degradation studies. They are closely related to the previously reported cyclotheonamide E, from which they differ in the N-acyl group of the alanyl side chain. Cyclotheonamides E, E2, and E3 were more active against thrombin than against trypsin.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Peptides, Cyclic / isolation & purification*
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Peptides, Cyclic / pharmacology
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Porifera / chemistry*
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Serine Proteinase Inhibitors / isolation & purification*
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Serine Proteinase Inhibitors / pharmacology
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Thrombin / antagonists & inhibitors*
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Trypsin Inhibitors / isolation & purification*
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Trypsin Inhibitors / pharmacology
Substances
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Peptides, Cyclic
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Serine Proteinase Inhibitors
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Trypsin Inhibitors
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cyclotheonamide E2
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cyclotheonamide E3
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Thrombin