The class
A fungal depsipeptide, SCH 58149, shows weak CETP inhibitory activity with an IC50 of 50 micromolar (Bioorg Med Chem Lett 1998)
Original title: A depsipeptide fungal metabolite inhibitor of cholesteryl ester transfer protein
Spectroscopic analysis of an organic extract from a fungal fermentation broth identified a new depsipeptide, SCH 58149, composed of three amino acids, phenylalanine, alanine, and leucine, plus a beta-hydroxy acid, 3-hydroxy-4-methyl octanoic acid. SCH 58149 exhibited weak activity against cholesterol ester transfer protein, with an IC50 of 50 micromolar, adding a structurally novel depsipeptide scaffold to the catalog of natural-product CETP inhibitors, albeit one with modest potency relative to other microbial leads.
Original 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.
Summary written by cetpinhibition.org from the published abstract; figures as published. Page updated 19 August 2026. Methods.