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Intramolecular Rearrangements in Peptide Derivatives of Anthranilic Acid
Author(s) -
Noguchi Junzo,
Kawai Megumi,
Hamada Masato
Publication year - 1974
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.197400010
Subject(s) - chemistry , anthranilic acid , racemization , peptide , hydrolysis , intramolecular force , peptide bond , residue (chemistry) , amide , acid hydrolysis , aqueous solution , stereochemistry , medicinal chemistry , amino acid , cyclic peptide , organic chemistry , combinatorial chemistry , biochemistry
The peptidylanthranilic acid ester is stable during the reactions leading to the elongation of peptides. However, when the ester is hydrolyzed, the amide bond of peptidylanthranilic acid is catalytically hydrolyzed at pH 7, owing to the effect of the free carboxyl group of the anthranilic residue, into peptide and anthranilic acid. In this reaction, no decomposition or significant racemization of peptide was observed, and the protected peptide was easily obtained. Only in the case of glycylanthraniloyl derivatives did the rearrangement into peptide and anthranilic acid occur in aqueous solution.