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Mass spectrometric determination of N‐terminal tryptophan and N‐terminal histidine in peptides
Author(s) -
Jayasimhulu K.,
Day R. A.
Publication year - 1980
Publication title -
biomedical mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 0306-042X
DOI - 10.1002/bms.1200070802
Subject(s) - chemistry , peptide , mass spectrometry , reagent , histidine , mass spectrum , dehydrogenation , schiff base , tryptophan , combinatorial chemistry , organic chemistry , stereochemistry , amino acid , chromatography , catalysis , biochemistry , enzyme
The successful utilization of Schiff base peptide ester derivatives in sequence elucidation of peptides by mass spectrometry led to the study of N‐terminal tryptophyl and histidyl peptides. We had earlier reported the formation of cyclization products when N ‐prolyl peptide esters had reacted with Schiff base forming reagents. We observed that the reaction of aldehydes with N ‐terminal tryptophyl peptide esters gave cyclization and subsequent dehydrogenation products which were found to be substituted β‐carbolines (9 H ‐pyrido(3,4‐ b )‐indoles) formed by Mannich type condensation. The molecular ion and many of the expected sequence identifying peaks were prominent in the mass spectra. The facile pyrolysis products of these peptide derivatives also indicated the presence of β‐carbolines and substituted β‐carbolines. In a similar fashion peptides with N‐terminal histidine gave 1 H ‐pyrido(4,5‐ c )imidazoles.