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Farnesyl protein transferase inhibitors targeting the catalytic zinc for enhanced binding.

Abstract：

:Successful efforts to make farnesyl transferase (FT) inhibitors with appropriately tethered ligands designed to interact with a catalytic zinc that exist in the enzyme have been realized. Thus, by introducing either a pyridylmethylamino or propylaminolimidazole amide moieties off the 2-position of the piperidine ring, FT inhibitors with activities in the picomolar range have been achieved as exemplified by compounds 12a and 12b. An X-ray structure of 11b bound to FT shows the enhanced activity is a result of interacting with the active-site zinc.

journal_name

Bioorg Med Chem Lett

journal_title

Bioorganic & medicinal chemistry letters

authors

Njoroge FG,Vibulbhan B,Pinto P,Strickland C,Kirschmeier P,Bishop WR,Girijavallabhan V

doi

10.1016/j.bmcl.2004.09.026

subject

Has Abstract

pub_date

2004-12-06 00:00:00

pages

5877-80

issue

23

eissn

0960-894X

issn

1464-3405

pii

S0960-894X(04)01138-2

journal_volume

14

pub_type

杂志文章

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