Non-thiol farnesyltransferase inhibitors: structure-activity relationships of benzophenone-based bisubstrate analogue farnesyltransferase inhibitors.
Investigations on the structure-activity relationships of benzophenone-based bisubstrate analogue farnesyltransferase inhibitors yielded a bisubstrate analogue farnesyltransferase inhibitor lacking any prenylic or peptidic substructures with nanomolar activity. This represents a considerable progress in comparison to those non-prenylic, non-peptidic bisubstrate analogue farnesyltransferase inhibitors we have described before which utilized AAX-peptidomimetic substructures different from the benzophenone since those inhibitors displayed activity only in the micromolar range.
Schlitzer
Martin
M
Institut für Pharmazeutische Chemie, Philipps-Universität Marburg, Marbacher Weg 6, D-35032 Marburg, Germany. schlitze@mailer.uni-marburg.de
Böhm
Markus
M
Sattler
Isabel
I
D019883:Alkyl and Aryl Transferases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D000577:Amides / Q000737:chemistry; D000970:Antineoplastic Agents / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D001577:Benzophenones / Q000737:chemistry* / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology; D051231:Farnesyltranstransferase; D005227:Fatty Acids / Q000737:chemistry; D013329:Structure-Activity Relationship; D015003:Yeasts / Q000201:enzymology
D000577:Amides; D000970:Antineoplastic Agents; D001577:Benzophenones; D004791:Enzyme Inhibitors; D005227:Fatty Acids; D019883:Alkyl and Aryl Transferases; D051231:Farnesyltranstransferase