A depsipeptide fungal metabolite inhibitor of cholesteryl ester transfer protein.
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.
Hegde
V R
VR
Schering Plough Research Institute, Kenilworth, NJ 07033, USA.
Dai
P
P
Patel
M
M
Das
P R
PR
Wang
S
S
Puar
M S
MS
D000164:Acremonium / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D002352:Carrier Proteins / Q000037:antagonists & inhibitors*; D053480:Cholesterol Ester Transfer Proteins; D002788:Cholesterol Esters / Q000378:metabolism*; D047630:Depsipeptides; D005285:Fermentation; D006023:Glycoproteins; D009682:Magnetic Resonance Spectroscopy; D010456:Peptides, Cyclic / Q000032:analysis / Q000302:isolation & purification / Q000494:pharmacology*; D016339:Spectrometry, Mass, Fast Atom Bombardment; D013056:Spectrophotometry, Ultraviolet
D000596:Amino Acids; D002352:Carrier Proteins; D053480:Cholesterol Ester Transfer Proteins; D002788:Cholesterol Esters; D047630:Depsipeptides; D006023:Glycoproteins; D010456:Peptides, Cyclic; C117555:SCH 58149