Design, synthesis and early structure–activity relationship of farnesyltransferase inhibitors which mimic both the peptidic and the prenylic substrate

M Schlitzer, M Böhm, I Sattler, HM Dahse

文献索引：Schlitzer, Martin; Boehm, Markus; Sattler, Isabel; Dahse, Hans-Martin Bioorganic and Medicinal Chemistry, 2000 , vol. 8, # 8 p. 1991 - 2006

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被引用次数: 30

摘要

Inhibition of the farnesylation of ras proteins has been identified as a promising target in tumor therapy. Only a few farnesyltransferase inhibitors are bisubstrate analogues displaying features of both substrates, the farnesylpyrophosphate and the C-terminal CAAX- tetrapeptide sequence of the ras protein. These known bisubstrate analogues consist of an AAX-tripeptide and a farnesyl residue connected through various linkers. We have ...