115014-77-2Relevant articles and documents
Lipase-catalyzed kinetic resolution of 2-aminocyclopentane- and 2-aminocyclohexanecarboxamides
Fitz, Monika,Lundell, Katri,Fueloep, Ferenc,Kanerva, Liisa T.
, p. 1129 - 1134 (2006)
Candida antarctica lipase B (CAL-B)-catalyzed N-acylation with 2,2,2-trifluoroethyl butanoate in solvent mixtures of tert-butyl methyl ether and tert-amyl alcohol was used to prepare all the enantiomers of cis- and trans-2-aminocyclopentane- and -cyclohexanecarboxamides. An unexpected change in enantiopreference, accompanied by low enantioselectivity, was observed when Pseudomonas cepacia lipase (cis-cyclohexane substrate) or C. antarctica lipase A (cis-cyclopentane and -cyclohexane substrates) replaced CAL-B.
Structure-based design and synthesis of phosphinate isosteres of phosphotyrosine for incorporation in Grb2-SH2 domain inhibitors. Part 1
Furet, Pascal,Caravatti, Giorgio,Denholm, Alastair A.,Faessler, Alex,Fretz, Heinz,Garcia-Echeverria, Carlos,Gay, Brigitte,Irving, Ed,Press, Neil J.,Rahuel, Joseph,Schoepfer, Joseph,Walker, Clive V.
, p. 2337 - 2341 (2007/10/03)
Based on X-ray crystal structure information, mono charged phosphinate isosteres of phosphotyrosine have been designed and incorporated in a short inhibitory peptide sequence of the Grb2-SH2 domain. The resulting compounds, by exploiting additional interactions, inhibit binding to the Grb2-SH2 domain as potently as the corresponding doubly charged (phosphonomethyl)phenylalanine analogue. (C) 2000 Elsevier Science Ltd.
An Efficient Synthesis of Stereoisomeric 2-(Substituted)-Aminocyclohexanecarboxamides
Pihlaja, Kalevi,Fueloep, Ferenc,Mattinen, Jorma,Bernath, Gabor
, p. 228 - 231 (2007/10/02)
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