Abstract
Extracts of the Floridian marine cyanobacterium Lyngbya cf. confervoides were found to deter feeding by reef fish and sea urchins (Diadema antillarum). This antifeedant activity may be a reflection of the secondary metabolite content, known to be comprised of many serine protease inhibitors. Further chemical and NMR spectroscopic investigation led us to isolate and structurally characterize a new serine protease inhibitor 1 that is formally derived from an intramolecular condensation of largamide D (2). The cyclization resulted in diminished activity, but to different extents against two serine proteases tested. This finding suggests that cyanobacteria can endogenously modulate the activity of their protease inhibitors.
Keywords:
Lyngbya; antifeedant activity; cyanobacteria; cyclodepsipeptides; serine protease inhibitors.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Atlantic Ocean
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Bacterial Toxins / chemistry
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Bacterial Toxins / isolation & purification
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Bacterial Toxins / pharmacology
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Chymotrypsin / antagonists & inhibitors
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Cyanobacteria / isolation & purification
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Cyanobacteria / metabolism*
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Depsipeptides / chemistry*
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Depsipeptides / isolation & purification
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Depsipeptides / pharmacology*
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Feeding Behavior / drug effects*
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Fishes
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Florida
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Marine Toxins / chemistry
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Marine Toxins / isolation & purification
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Marine Toxins / pharmacology
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Molecular Structure
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Nuclear Magnetic Resonance, Biomolecular
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Osmolar Concentration
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Pancreatic Elastase / antagonists & inhibitors
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Sea Urchins
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Seawater / microbiology
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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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Spectrometry, Mass, Electrospray Ionization
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Tandem Mass Spectrometry
Substances
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Bacterial Toxins
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Depsipeptides
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Marine Toxins
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Serine Proteinase Inhibitors
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largamide D
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Chymotrypsin
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Pancreatic Elastase