Eight new components of terpendoles E to L were isolated and characterized from the culture broth of Albophoma yamanashiensis using a different production medium. All the structures were elucidated by spectroscopic analyses including various NMR experiments, indicating that all the terpendoles have the same indoloditerpene core as terpendoles A to D. Terpendoles J, K and L showed the moderate inhibition against acyl-CoA: cholesterol acyltransferase (ACAT) activity with IC50 values of 38.8, 38.0 and 32.4 microM in rat liver microsomes, respectively. But terpendoles E-I showed weak activities (IC50 145-388 microM).
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.7164/antibiotics.48.793 | DOI Listing |
J Antibiot (Tokyo)
August 1995
Research Center for Biological Function, Kitasato Institute, Kitasato University, Tokyo, Japan.
Eight new components of terpendoles E to L were isolated and characterized from the culture broth of Albophoma yamanashiensis using a different production medium. All the structures were elucidated by spectroscopic analyses including various NMR experiments, indicating that all the terpendoles have the same indoloditerpene core as terpendoles A to D. Terpendoles J, K and L showed the moderate inhibition against acyl-CoA: cholesterol acyltransferase (ACAT) activity with IC50 values of 38.
View Article and Find Full Text PDFJ Antibiot (Tokyo)
January 1995
Research Center for Biological Function, Kitasato Institute, Tokyo, Japan.
Structures of terpendoles A, B, C and D, novel acyl-CoA: cholesterol acyltransferase (ACAT) inhibitors, were determined by spectroscopic studies. All terpendoles consist of diterpene and indole moieties in common. Terpendoles A, C and D possess an additional isoprenyl unit via oxygen atom(s) of their diterpene moieties.
View Article and Find Full Text PDFJ Antibiot (Tokyo)
January 1995
Research Center for Biological Function, Kitasato Institute, Tokyo, Japan.
A series of new acyl-CoA: cholesterol acyltransferase (ACAT) inhibitors termed terpendoles were isolated from the culture broth of a fungal strain FO-2546 which was proposed to belong to a new genus designated as Albophoma yamanashiensis. Among four structurally related terpendoles, terpendole C showed the most potent ACAT inhibitory activity with an IC50 value of 2.1 microM in an in vitro enzyme assay, followed by terpendoles D (IC50: 3.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!