Mass Spectrometric (FAB) Study of Aspartic Acid Side Reactions in Peptide Synthesis
作者:
K. Jankowskia,
D. Caudina,
P.Pham Van Chuoncb,
期刊:
Spectroscopy Letters
(Taylor Available online 1987)
卷期:
Volume 20,
issue 3
页码: 255-284
ISSN:0038-7010
年代: 1987
DOI:10.1080/00387018708081548
出版商: Taylor & Francis Group
数据来源: Taylor
摘要:
We have been interested in the synthesis of branched peptides, by grafting an amine, eg histamine, to the carboxylic group of aspartic acid side chain of Boc-β Ala-Trp-Met-Asp-Phe-NH2also called Pentagastrin (or α-PG). Depending on the coupling conditions used, the main product obtained might be either the wanted derivative or a side-product identified a6 amino-succinyl-pentagastrin (or ASC-PG). Acid or base treatment of this product cleaved the amino-succinyl ring and yielded either α-PG or/and (β-Aspartyl)4-PC or β-PG. Amino-succinylation being a general problem in peptide synthesis of aspartyl residue containing peptides, synthesis of α-PG, β-PG, Asc-PG and their corresponding C-terminal dipeptide amides were performed to be analyzed by mass spectroscopy.
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