Abstract
A series of acyclic, truncated microcystin analogues, comprised of the dienic beta-amino acid (Adda) and up to four additional amino acids characteristic of the parent toxin, was synthesized and screened for activity as inhibitors of PP1 and PP2A. Despite a recent report to the contrary for a microcystin-derived tetrapeptide degradation product, none approaches the potency of microcystin itself.
Publication types
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Comparative Study
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bacterial Toxins
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Enzyme Inhibitors / chemistry*
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Enzyme Inhibitors / pharmacology*
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Inhibitory Concentration 50
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Isoenzymes
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Marine Toxins
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Microcystins
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Oligopeptides / chemical synthesis
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Oligopeptides / pharmacology
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Peptides, Cyclic / chemistry*
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Peptides, Cyclic / pharmacology*
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Phosphoprotein Phosphatases / antagonists & inhibitors*
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Structure-Activity Relationship
Substances
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Bacterial Toxins
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Enzyme Inhibitors
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Isoenzymes
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Marine Toxins
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Microcystins
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Oligopeptides
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Peptides, Cyclic
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microcystin
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Phosphoprotein Phosphatases
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cyanoginosin LR