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- W1997923397 abstract "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." @default.
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- W1997923397 date "1996-02-01" @default.
- W1997923397 modified "2023-09-23" @default.
- W1997923397 title "New synthesis of D,L-fmoc protected 4- phosphonomethylphenylalanine derivatives and their enzymatic resolution" @default.
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- W1997923397 doi "https://doi.org/10.1016/0040-4020(95)01003-3" @default.
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