Non-thiol farnesyltransferase inhibitors: utilization of the far aryl binding site by arylthienylacryloylaminobenzophenones.
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.
Mitsch
Andreas
A
Institut für Pharmazeutische Chemie, Philipps-Universität Marburg, Marburg, Germany.
Altenkämper
Mirko
M
Sattler
Isabel
I
Schlitzer
Martin
M
D000178:Acrylamides / Q000737:chemistry*; D019883:Alkyl and Aryl Transferases / Q000037:antagonists & inhibitors* / Q000737:chemistry*; D001577:Benzophenones / Q000737:chemistry*; D001665:Binding Sites; D051231:Farnesyltranstransferase; D013329:Structure-Activity Relationship; D013876:Thiophenes / Q000737:chemistry*
D000178:Acrylamides; D001577:Benzophenones; D013876:Thiophenes; D019883:Alkyl and Aryl Transferases; D051231:Farnesyltranstransferase