Stigonemapeptin, an Ahp-containing depsipeptide with elastase inhibitory activity from the bloom-forming freshwater cyanobacterium Stigonema sp

J Nat Prod. 2012 Apr 27;75(4):807-11. doi: 10.1021/np300150h. Epub 2012 Apr 6.

Abstract

Stigonemapeptin (1), a depsipeptide containing an Ahp (3-amino-6-hydroxy-2-piperidone) residue, was isolated from a bloom sample of the freshwater cyanobacterium Stigonema sp. collected from North Nokomis Lake in the Highland Lake District of northern Wisconsin. The planar structure was determined by 1D and 2D NMR experiments as well as HRESIMS analysis. The absolute configurations of the amino acids were determined using the advanced Marfey's method after acid hydrolysis. Stigonemapeptin (1), characterized by the presence of the Ahp residue, also contained the modified amino acids Abu (2-amino-2-butenoic acid) and N-formylated Pro. Stigonemapeptin (1) showed in vitro elastase and chymotrypsin inhibitory activity, with IC(50) values of 0.26 and 2.93 μM, respectively.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acids / analysis
  • Animals
  • Cattle
  • Chymotrypsin / antagonists & inhibitors
  • Cyanobacteria / chemistry*
  • Depsipeptides / chemistry
  • Depsipeptides / isolation & purification*
  • Depsipeptides / pharmacology*
  • Fresh Water / microbiology
  • Inhibitory Concentration 50
  • Molecular Structure
  • Nuclear Magnetic Resonance, Biomolecular
  • Pancreas / enzymology
  • Pancreatic Elastase / antagonists & inhibitors*
  • Piperidones / chemistry
  • Swine
  • Wisconsin

Substances

  • 3-amino-6-hydroxy-2-piperidone
  • Amino Acids
  • Depsipeptides
  • Piperidones
  • stigonemapeptin
  • Chymotrypsin
  • Pancreatic Elastase