Lyngbyastatins 8-10, elastase inhibitors with cyclic depsipeptide scaffolds isolated from the marine cyanobacterium Lyngbya semiplena.
Investigation of an extract from the marine cyanobacterium Lyngbya semiplena, collected in Tumon Bay, Guam, led to the identification of three new cyclodepsipeptides, lyngbyastatins 8-10 (1-3). The structures of 1-3 were determined by NMR, MS, ESIMS fragmentation and chemical degradation. Compounds 1-3 are closely related to lyngbyastatins 4-7. Like the latter compounds, we found 1-3 to inhibit porcine pancreatic elastase, with IC(50) values of 123 nM, 210 nM and 120 nM, respectively.
Kwan
Jason C
JC
Department of Medicinal Chemistry, University of Florida, 1600 SW Archer Road, Gainesville, FL 32610, USA. jkwan@ufl.edu
Taori
Kanchan
K
Paul
Valerie J
VJ
Luesch
Hendrik
H
D000818:Animals; D000458:Cyanobacteria / Q000737:chemistry*; D047630:Depsipeptides / Q000737:chemistry / Q000302:isolation & purification*; D004305:Dose-Response Relationship, Drug; D006141:Guam; D009682:Magnetic Resonance Spectroscopy; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors*; D021241:Spectrometry, Mass, Electrospray Ionization; D013552:Swine
D047630:Depsipeptides; C550264:lyngbyastatin 10; C550262:lyngbyastatin 8; C550263:lyngbyastatin 9; D010196:Pancreatic Elastase