Linearized and truncated microcystin analogues as inhibitors of protein phosphatases 1 and 2A.
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.
Gulledge
Brian M
BM
Department of Chemistry, University of California at Irvine, CA 92697, USA.
Aggen
James B
JB
Chamberlin
A Richard
AR
D001427:Bacterial Toxins; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D020128:Inhibitory Concentration 50; D007527:Isoenzymes; D008387:Marine Toxins; D052998:Microcystins; D009842:Oligopeptides / Q000138:chemical synthesis / Q000494:pharmacology; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000494:pharmacology*; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors*; D013329:Structure-Activity Relationship
D001427:Bacterial Toxins; D004791:Enzyme Inhibitors; D007527:Isoenzymes; D008387:Marine Toxins; D052998:Microcystins; D009842:Oligopeptides; D010456:Peptides, Cyclic; C078588:microcystin; D010749:Phosphoprotein Phosphatases; C057862:cyanoginosin LR