Kempopeptins A and B, serine protease inhibitors with different selectivity profiles from a marine cyanobacterium, Lyngbya sp

J Nat Prod. 2008 Sep;71(9):1625-9. doi: 10.1021/np8002172. Epub 2008 Aug 12.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Cattle
  • Chymotrypsin / antagonists & inhibitors
  • Cyanobacteria / chemistry*
  • Depsipeptides / chemistry
  • Depsipeptides / isolation & purification*
  • Depsipeptides / pharmacology*
  • Florida
  • Inhibitory Concentration 50
  • Marine Biology
  • Molecular Structure
  • Nuclear Magnetic Resonance, Biomolecular
  • Pancreas / enzymology
  • Pancreatic Elastase / antagonists & inhibitors
  • Serine Proteinase Inhibitors / chemistry
  • Serine Proteinase Inhibitors / isolation & purification*
  • Serine Proteinase Inhibitors / pharmacology*
  • Swine

Substances

  • Depsipeptides
  • Serine Proteinase Inhibitors
  • kempopeptin A
  • kempopeptin B
  • Chymotrypsin
  • Pancreatic Elastase