New fungal metabolite geranylgeranyltransferase inhibitors with antifungal activity.

Published

Journal Article

Geranylgeranyltransferase I (GGTase I) catalyzes the post-translational transfer of lyophilic diterpenoid geranylgeranyl to the cysteine residue of proteins terminating with a CaaX motif such as Rho1p and Cdc42p. It has been shown that GGTase I activity is essential for viability of Saccharomyces cerevisiae and hence its inhibition is a potential antifungal target. From natural product screening, a number of azaphilones including one novel analog were isolated as broad-spectrum inhibitors of GGTase I. Isolation, structure elucidation, GGTase I inhibitory activities and antifungal activities of these compounds are described.

Full Text

Duke Authors

Cited Authors

  • Singh, SB; Kelly, R; Guan, Z; Polishook, JD; Domrowski, AW; Collado, J; Gonzalez, A; Pelaez, F; Register, E; Kelly, TM; Bonfiglio, C; Williamson, JM

Published Date

  • December 2005

Published In

Volume / Issue

  • 19 / 8

Start / End Page

  • 739 - 747

PubMed ID

  • 16317828

Pubmed Central ID

  • 16317828

Electronic International Standard Serial Number (EISSN)

  • 1478-6427

International Standard Serial Number (ISSN)

  • 1478-6419

Digital Object Identifier (DOI)

  • 10.1080/1478641042000334715

Language

  • eng