Premium
Non‐Thiol Farnesyltransferase Inhibitors: Utilization of the Near Aryl Binding Site by 5‐Arylacetylaminobenzophenones
Author(s) -
Mitsch Andreas,
Böhm Markus,
Sattler Isabel,
Schlitzer Martin
Publication year - 2004
Publication title -
archiv der pharmazie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 61
eISSN - 1521-4184
pISSN - 0365-6233
DOI - 10.1002/ardp.200300843
Subject(s) - farnesyltransferase , thiol , chemistry , aryl , farnesyl diphosphate farnesyltransferase , binding site , farnesyltransferase inhibitor , combinatorial chemistry , stereochemistry , pharmacology , biochemistry , enzyme , organic chemistry , prenylation , medicine , alkyl
We recently described two novel aryl binding sites of farnesyltransferase. The arylacetyl residue was designed as an appropriate substituent for our benzo‐phenone‐based AAX‐peptidomimetic compound capable of occupying the near aryl binding site which is located next to the catalytic zinc ion. Non‐thiol farnesyl‐transferase inhibitors with micromolar to submicromolar activity were obtained.