220903-35-5Relevant academic research and scientific papers
Rhodium-catalyzed intramolecular hydroacylation of 1,2-disubstituted alkenes for the synthesis of 2-substituted indanones
Yuan, Jing,Liu, Chong,Chen, Yan,Zhang, Zhenfeng,Yan, Deyue,Zhang, Wanbin
, p. 269 - 277 (2018/12/05)
The intramolecular hydroacylation of 1,2-disubstituted alkenes was considered to be a challenging task due to the side reactions resulted from the lack of additional substituent at 1-position and the low activity caused by the steric hindrance of substituent at 2-position, and an asymmetric version has not been considered possible due to problems associated with the racemization of the products. We have partially solved these problems. Catalyzed by an activated diphosphine-Rh complex and reacted in a selected dihalogenated solvent, the intramolecular hydroacylation of o-(2-arylvinyl)benzaldehydes provided the corresponding 2-aryl-1-indanones in high yields, and its asymmetric variant using o-(2-alkylvinyl)benzaldehydes afforded chiral 2-alkyl-1-indanones in high yields and with moderate enantioselectivities.
Synthesis and in vitro evaluation of the farnesyltransferase inhibitor pepticinnamin E
Hinterding, Klaus,Hagenbuch, Patrizia,Re?tey, Janos,Waldmann, Herbert
, p. 227 - 236 (2007/10/03)
The farnesyltransferase inhibitor pepticinnamin E was synthesized and shown to have the S configuration at the central, non-proteinogenic amino acid. Using a recombinant yeast farnesyltransferase the biological activity of the natural product and structur
Synthesis and in vitro evaluation of the Ras farnesyltransferase inhibitor pepticinnamin E
Hinterding, Klaus,Hagenbuch, Patrizia,Retey, Janos,Waldmann, Herbert
, p. 1236 - 1239 (2007/10/03)
A modularly built bisubstrate inhibitor, the natural product pepticinnamin E (shown on the right) was synthesized for the first time. In the case of in vitro assays it inhibits the enzyme farnesyltransferase with respect to both the peptide substrate and farnesylpyrophosohate (K1 = 30 and 8 μM, respectively). The inhibitory activity is decisively influenced by the central tripeptide unit and the absolute configuration of the non-proteinogenic amino acid incorporated therein.
