Corticatic acids D and E, polyacetylenic geranylgeranyltransferase type I inhibitors, from the marine sponge Petrosia corticata
Related Experiment Video
Updated: Sep 29, 2026

Overexpression and Purification of Human Cis-prenyltransferase in Escherichia coli
Published on: August 3, 2017
Shinichi Nishimura1, Shigeki Matsunaga, Mitsuyoshi Shibazaki
1Laboratory of Aquatic Natural Products Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Japan.
Abstract:
Two new polyacetylenic acids, corticatic acids D (2) and E (3), have been isolated from the marine sponge Petrosia corticata along with the known corticatic acid A (1) as geranylgeranyltransferase type I (GGTase I) inhibitors. Their structures were elucidated on the basis of spectroscopic and chemical methods. Compounds 1-3 inhibited GGTase I from Candida albicans with IC(50) values of 1.9-7.3 microM.
Related Concept Videos
Antifungal Agents
Lipids as Anchors
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Phosphoinositides and PIPs
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...

