Abstract
Two cyclodepsipeptides named kempopeptins A (1) and B (2) were isolated from a collection of a Floridian marine cyanobacterium, Lyngbya sp., that had previously afforded the structurally related potent elastase inhibitors lyngbyastatin 7 and somamide B. The structures of 1 and 2 were elucidated mainly by 1D and 2D NMR spectroscopy, and the absolute configuration was established by chiral HPLC and Marfey's analysis of the degradation products. Kempopeptin A (1) exhibited an IC50 against elastase of 0.32 microM and against chymotrypsin of 2.6 microM, while kempopeptin B (2) inhibited trypsin with an IC50 of 8.4 microM.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Animals
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Cattle
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Chymotrypsin / antagonists & inhibitors
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Cyanobacteria / chemistry*
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Depsipeptides / chemistry
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Depsipeptides / isolation & purification*
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Depsipeptides / pharmacology*
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Florida
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Inhibitory Concentration 50
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Marine Biology
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Molecular Structure
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Nuclear Magnetic Resonance, Biomolecular
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Pancreas / enzymology
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Pancreatic Elastase / antagonists & inhibitors
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Serine Proteinase Inhibitors / chemistry
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Serine Proteinase Inhibitors / isolation & purification*
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Serine Proteinase Inhibitors / pharmacology*
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Swine
Substances
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Depsipeptides
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Serine Proteinase Inhibitors
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kempopeptin A
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kempopeptin B
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Chymotrypsin
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Pancreatic Elastase