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Non‐Thiol Farnesyltransferase Inhibitors: Utilization of the Far Aryl Binding Site by Arylthienylacryloylaminobenzophenones
Author(s) -
Mitsch Andreas,
Altenkämper Mirko,
Sattler Isabel,
Schlitzer Martin
Publication year - 2005
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.200400886
Subject(s) - farnesyltransferase , chemistry , thiol , aryl , farnesyl diphosphate farnesyltransferase , farnesyltransferase inhibitor , stereochemistry , combinatorial chemistry , pharmacology , biochemistry , enzyme , organic chemistry , medicine , prenylation , alkyl
We recently described two novel aryl binding sites of farnesyltransferase. The 4‐ and 5‐arylsubstituted thienylacryloyl moieties turned out as appropriate substituents for our benzophenone‐based AAX—peptidomimetic capable for occupying the far aryl binding site.