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Synthesis of β‐pyrazinyl‐ L ‐alanine (Paa) and of peptide derivatives
Author(s) -
Petermann Claudia,
Fauchère JeanLuc
Publication year - 1983
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19830660518
Subject(s) - chemistry , pentapeptide repeat , steric effects , peptide , leucine , hydrolysis , amino acid , stereochemistry , peptide synthesis , phenylalanine , organic chemistry , biochemistry
The title compound was prepared via a malonic ester synthesis starting with α‐chloromethylpyrazine [2], and ending, after an asymmetric enzymatic hydrolysis of the racemic N ‐acetyl‐β‐2‐pyrazinylalanine to the L ‐form of the new amino acid. The optical purity was ascertained by 1 H‐NMR analysis at 360 MHz of the diastereoisomeric dipeptides L ‐pyrazinylalanine‐ L ‐leucine and D ‐pyrazinylalanine‐ L ‐leucine. Hydrophobic, steric and electronic parameters for its side chain were also estimated, which can be useful for the quantitative study of structure‐activity relationships of biologically active peptide derivatives. The new amino acid could be introduced in the place of phenylalanine in the enkephalin‐like pentapeptide [ D ‐alanyl 2 , leucine 5 ]enkephalin, thus showing good stability towards the classical methods of peptide synthesis.