2. Academic Validation
  3. Amide-substituted farnesylcysteine analogs as inhibitors of human isoprenylcysteine carboxyl methyltransferase

Amide-substituted farnesylcysteine analogs as inhibitors of human isoprenylcysteine carboxyl methyltransferase

  • Bioorg Med Chem Lett. 2006 Aug 15;16(16):4420-3. doi: 10.1016/j.bmcl.2006.05.029.
James L Donelson 1,  Heather B Hodges,  Daniel D Macdougall,  Brian S Henriksen,  Christine A Hrycyna,  Richard A Gibbs
Affiliations

Affiliation

  • 1 Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907, USA.
PMID: 16777414 DOI: 10.1016/j.bmcl.2006.05.029
Abstract

N-Acetyl-S-farnesyl-L-cysteine (AFC) is the minimal substrate for the Enzyme isoprenylcysteine carboxyl methyltransferase (ICMT). A series of amide-modified farnesylcysteine analogs were synthesized and screened against human ICMT. From a 23-membered library of compounds, six inhibitors were identified and evaluated further. The adamantyl derivative 7c was the most potent inhibitor with an IC(50) of 12.4 microM.

Figures
Products
  • Cat. No.
    Product Name
    Description
    Target
    Research Area
  • HY-149730
    ICMT抑制剂
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