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Non‐thiol Farnesyltransferase Inhibitors: Utilization of the Far Aryl Binding Site by 5‐Cinnamoylaminobenzophenones
Author(s) -
Mitsch Andreas,
Wißner Pia,
Böhm Markus,
Silber Katrin,
Klebe Gerhard,
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.200400871
Subject(s) - farnesyltransferase , aryl , benzophenone , chemistry , farnesyl diphosphate farnesyltransferase , peptidomimetic , substituent , stereochemistry , binding site , combinatorial chemistry , organic chemistry , biochemistry , enzyme , prenylation , peptide , alkyl
We recently described two novel aryl binding sites of farnesyltransferase. In this study, the cinnamoyl residue was designed as an appropriate substituent for our benzophenone‐based AAX‐peptidomimetic compound capable of occupying the far aryl binding site.