Kempopeptins A and B, serine protease inhibitors with different selectivity profiles from a marine cyanobacterium, Lyngbya sp.
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.
Taori
Kanchan
K
Department of Medicinal Chemistry, University of Florida, 1600 SW Archer Road, Gainesville, Florida 32610, USA.
Paul
Valerie J
VJ
Luesch
Hendrik
H
D000818:Animals; D002417:Cattle; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D000458:Cyanobacteria / Q000737:chemistry*; D047630:Depsipeptides / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*; D005431:Florida; D020128:Inhibitory Concentration 50; D008386:Marine Biology; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D010179:Pancreas / Q000201:enzymology; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*; D013552:Swine
D047630:Depsipeptides; D015842:Serine Proteinase Inhibitors; C532712:kempopeptin A; C532713:kempopeptin B; D002918:Chymotrypsin; D010196:Pancreatic Elastase