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Potent and selective farnesyl transferase inhibitors.

Abstract：

:We recently described a novel series of CA(1)A(2)X peptidomimetics as farnesyl transferase inhibitors (FTIs). These compounds possess an N-(4-piperidinyl)benzamide scaffold mimicking A(1)A(2) residue. Extensive exploration of structure--activity relationships revealed that replacement of cysteine by substituted benzylimidazoles provided nanomolar FTIs with in vitro activities (18e, IC(50) = 4.60 nM on isolated enzyme, EC(50) = 20.0 nM for growth inhibition on a tumor cell line). The molecular docking of 18e and 19e in the active site of the enzyme provided details of key interactions with the protein and showed that the methionine or phenylalanine residue fits into the aryl binding site.

journal_name

J Med Chem

journal_title

Journal of medicinal chemistry

authors

Millet R,Domarkas J,Houssin R,Gilleron P,Goossens JF,Chavatte P,Logé C,Pommery N,Pommery J,Hénichart JP

doi

10.1021/jm030502y

keywords:

subject

Has Abstract

pub_date

2004-12-30 00:00:00

pages

6812-20

issue

27

eissn

0022-2623

issn

1520-4804

journal_volume

47

pub_type

杂志文章

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