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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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