Abstract

This paper reports testing 15 polyether triterpenes with a squalene carbon skeleton for inhibitory effects on type 2A protein phosphatase. Two compounds, 16-hydroxydehydrothyrsiferol 10 and thyrsenol B 14, exhibited significant inhibitory action at a concentration of 10 microM. Comparison with thyrsiferyl-23-acetate 1 showed that a similar spatial disposition for the hydroxy group around C-15 or C-16 was the structural feature shared by these metabolites.