138228-86-1Relevant articles and documents
New synthesis of D,L-Fmoc protected 4-phosphonomethylphenylalanine derivatives and their enzymatic resolution
Baczko, Krystyna,Liu, Wang-Qing,Roques, Bernard P.,Garbay-Jaureguiberry, Christiane
, p. 2021 - 2030 (1996)
A new synthesis of N-Fmoc-4-phosphonomethyl-D,L-phenylalanine protected under di-tert-butyl or dimethyl phosphonate forms (Fmoc-Pmp(OR)2), suitable for solid phase peptide synthesis is described. Resolution of these hydrolytically stable analogs of O-phosphotyrosine was tried either by fractional recrystallization of diastereoisomeric salts or by using the subtilisin Carlsberg esterase. Only the enzymatic resolution of ethyl 4-[(dimethylphosphono)methyl]-D,L-phenylalaninate succeeded. These results are discussed by comparison with the literature data. The L and D amino acids were used to prepare separately, through solid-phase peptide synthesis, followed by deprotection of dimethylphosphonate group by trimethylsilyliodide (TMSI) in acetonitrile, the L and D isomers of Glu-Asp-Val-Pmp-Glu-Asn-Leu-His-Thr, a peptide corresponding to a potentially phosphorylated site of the phosphatase PTP 1C.
Phosphonoalkyl phenylalanine compounds suitably protected for use in peptide synthesis
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, (2008/06/13)
There are disclosed novel compounds of the formula: STR1 wherein, x is --CH2 --, --CHF--, --CF2, --CHOH-- or --C(O)--; R6 is hydrogen, benzyl, pentafluorophenyl, nitrophenyl, 1-benzotriazolyl or 1-succinimidoyl; Fmoc is 9-
