A depsipeptide fungal metabolite inhibitor of cholesteryl ester transfer protein

Bioorg Med Chem Lett. 1998 Jun 2;8(11):1277-80. doi: 10.1016/s0960-894x(98)00224-8.

Abstract

The organic extract of the fermentation broth of a fungus was found to contain a depsipeptide SCH 58149 (1), containing three amino acids and a beta-hydroxy acid, by spectroscopic studies. The amino acids were phenyl alanine, alanine and leucine and the beta-hydroxy acid is 3-hydroxy-4-methyl octanoic acid. SCH 58149 exhibited weak activity against cholesterol ester transfer protein (CETP) with an IC50 of 50 microM.

MeSH terms

  • Acremonium / metabolism*
  • Amino Acids / analysis
  • Carrier Proteins / antagonists & inhibitors*
  • Cholesterol Ester Transfer Proteins
  • Cholesterol Esters / metabolism*
  • Depsipeptides*
  • Fermentation
  • Glycoproteins*
  • Magnetic Resonance Spectroscopy
  • Peptides, Cyclic / analysis
  • Peptides, Cyclic / isolation & purification
  • Peptides, Cyclic / pharmacology*
  • Spectrometry, Mass, Fast Atom Bombardment
  • Spectrophotometry, Ultraviolet

Substances

  • Amino Acids
  • Carrier Proteins
  • Cholesterol Ester Transfer Proteins
  • Cholesterol Esters
  • Depsipeptides
  • Glycoproteins
  • Peptides, Cyclic
  • SCH 58149