A previously described cembranolide diterpene from Lobophytum cristagalli was identified as a potent (IC50 0.15 μM) inhibitor of farnesyl protein transferase (FPT). The compound showed selectivity for FPT as compared to the closely related enzyme geranylgeranyl protein transferase-1 (IC50 5.3 μM). Kinetic evaluation suggests that this compound competes with the protein/peptide farnesyl acceptor substrate, and not with farnesyl pyrophosphate for inhibition of FPT.
This manuscript is an author version with the final publication available at http://www.sciencedirect.com/science/journal/0960894X and may be cited as: Coval, S. J., Patton, R. W., Petrin, J. M., James, L., Rothofsky, M. L., Lin, S. L., Patel, M., Reed, J. K., McPhail, A. T., & Bishop, W. R. (1996). A cembranolide diterpene farnesyl protein transferase inhibitor from the marine soft coral Lobophytum cristagalli. Bioorganic & Medicinal Chemistry Letters, 6(7), 909-912. doi:10.1016/0960-894X(96)00142-4
Florida Atlantic University. Harbor Branch Oceanographic Institute contribution #1131.