92136-16-8Relevant academic research and scientific papers
Different amino acid replacements in CAAX-tetrapeptide based peptidomimetic farnesyltransferase inhibitors
Schlitzer, Martin,Sattler, Isabel,Dahse, Hans-Martin
, p. 124 - 132 (2007/10/03)
In a series of CAAX-tetrapeptide based farnesyltransferase inhibitors it has been shown that the central AA-dipeptide can be replaced by tranexamic acid, 4-aminobenzenesulfonic acid, and 3-amino-N-(2,3- dimethylphenyl)benzenesulfonamide, respectively, yielding inhibitors active in the low micromolar range. Lipophilic derivatives of these compounds showed moderate antiproliferative activity against different tumor cell lines. A promising class of peptidomimetic farnesyltransferase inhibitors was discovered through the replacement of the terminal AAX motif of the CAAX- tetrapeptide by 2-acylamino-5-aminobenzophenones.
