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Fragmentation and sequencing of cyclic peptides by matrix‐assisted laser desorption/ionization post‐source decay mass spectrometry
Author(s) -
Schilling Birgit,
Wang Wei,
McMurray John S.,
Medzihradszky Katalin F.
Publication year - 1999
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/(sici)1097-0231(19991115)13:21<2174::aid-rcm771>3.0.co;2-k
Subject(s) - chemistry , cyclic peptide , fragmentation (computing) , mass spectrometry , matrix assisted laser desorption/ionization , peptide , mass spectrum , protein mass spectrometry , amino acid , peptide sequence , desorption , chromatography , tandem mass spectrometry , biochemistry , organic chemistry , adsorption , computer science , gene , operating system
A series of synthetic cyclic decapeptides and other smaller cyclic peptides were analyzed using matrix‐assisted laser desorption/ionization time‐of‐flight (MALDI‐TOF) mass spectrometry. The investigated compounds were cyclized in a head‐to‐tail manner and contained non‐proteinaceous amino acids, such as D ‐phenylalanine, D , L ‐4‐carboxyphenylalanine, ϵ‐aminocaproic acid, and γ‐aminobutyric acid, and were synthesized in a program to develop inhibitors of pp60 c‐src (Src), a tyrosine kinase that is involved in signal transduction and growth regulation. Post‐source decay (PSD) spectra of the cyclic peptides featured abundant sequence ions. Two preferential ring opening reactions were detected resulting in linear fragment ions with an N‐terminus of proline and a C‐terminus of glutamic acid, respectively. MALDI‐PSD spectra even permitted de novo sequencing of some cyclic peptides. Systematic studies on cyclic peptides using this method of fragmentation have not been reported to date. This work presents an easy mass spectrometric method, MALDI‐PSD, for the characterization and identification of cyclic peptides. Copyright © 1999 John Wiley & Sons, Ltd.