Ontology highlight
ABSTRACT:
SUBMITTER: Majmudar JD
PROVIDER: S-EPMC3401633 | biostudies-literature | 2011 May
REPOSITORIES: biostudies-literature
Majmudar Jaimeen D JD Hahne Kalub K Hrycyna Christine A CA Gibbs Richard A RA
Bioorganic & medicinal chemistry letters 20110122 9
Human isoprenylcysteine carboxyl methyltransferase (hIcmt) is a promising anticancer target as it is important for the post-translational modification of oncogenic Ras proteins. We herein report the synthesis and biochemical activity of 41 farnesyl-cysteine based analogs versus hIcmt. We have demonstrated that the amide linkage of a hIcmt substrate can be replaced by a sulfonamide bond to achieve hIcmt inhibition. The most potent sulfonamide-modified farnesyl cysteine analog was 6ag with an IC(5 ...[more]