Non-thiol farnesyltransferase inhibitors: utilization of the far aryl binding site by 5-cinnamoylaminobenzophenones.
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.
Mitsch
Andreas
A
Institut für Pharmazeutische Chemie, Philipps-Universität Marburg, Germany.
Wissner
Pia
P
Böhm
Markus
M
Silber
Katrin
K
Klebe
Gerhard
G
Sattler
Isabel
I
Schlitzer
Martin
M
D019883:Alkyl and Aryl Transferases / Q000037:antagonists & inhibitors*; D001577:Benzophenones / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D001665:Binding Sites; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D051231:Farnesyltranstransferase; D008958:Models, Molecular; D018716:Molecular Mimicry; D015394:Molecular Structure; D013329:Structure-Activity Relationship; D015003:Yeasts / Q000201:enzymology
D001577:Benzophenones; D004791:Enzyme Inhibitors; D019883:Alkyl and Aryl Transferases; D051231:Farnesyltranstransferase