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Probing the isoprenylcysteine carboxyl methyltransferase (Icmt) binding pocket: sulfonamide modified farnesyl cysteine (SMFC) analogs as Icmt inhibitors.

Abstract：

: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(50) of 8.8±0.5 μM for hIcmt.

journal_name

Bioorg Med Chem Lett

journal_title

Bioorganic & medicinal chemistry letters

authors

Majmudar JD,Hahne K,Hrycyna CA,Gibbs RA

doi

10.1016/j.bmcl.2011.01.078

subject

Has Abstract

pub_date

2011-05-01 00:00:00

pages

2616-20

issue

9

eissn

0960-894X

issn

1464-3405

pii

S0960-894X(11)00101-6

journal_volume

21

pub_type

杂志文章

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