The mass spectrometric sequence determination of amino acid residues in cyclosporins using fast atom bombardment, collisionally activated dissociations in the first field-free region and linked B/E scan is described. The general fragmentation scheme was derived from the spectra of cyclosporins A,B,C
Distinguishing isobaric amino acids in sequence analysis of cyclosporins by fast atom bombardment and linked-scan mass spectrometry
✍ Scribed by Vladimír Havlíček; Alexandr Jegorov; Petr Sedmera; Winfried Wagner-Redeker; Miroslav Ryska
- Publisher
- John Wiley and Sons
- Year
- 1995
- Tongue
- English
- Weight
- 728 KB
- Volume
- 30
- Category
- Article
- ISSN
- 1076-5174
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✦ Synopsis
Abstract
An analytical protocol suggested previously for the mass spectrometric sequence analysis of cyclosporins was extended by addition of methods for discrimination among isobaric amino acids differing either in the nature of the side‐chain or N‐substitution. The former goal was achieved by comparison of B/E linked‐scan mass spectra of corresponding collisionally activated immonium ions with those of standard amino acids and the latter by comparison of B/E fragment ion spectra of [M + H]^+^ and [M~d~ + ^2^H]^+^ ions. The use of the improved protocol is illustrated by the structure elucidation of a novel natural cyclosporin, [Leu^9^]CS.
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In this paper, we have shown that it is possible to differentiate an aspartic acid residue from its p-aspartic acid isomer in dipeptides according to the characteristic fragmentation pathways, i.e. specific immonium ion formation and cleavages involving side-chain atoms.
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