Electron Transfer Dissociation of Amide Nitrogen Methylated Polypeptide Cations

Unmodified and amide nitrogen methylated peptide cations were reacted with azobenzene radical anions to study the utility of electron transfer dissociation (ETD) in analyzing N-methylated peptides. We show that methylation of the amide nitrogen has no deleterious effects on the ETD process. As a res...

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Bibliographic Details
Published in:Journal of the American Society for Mass Spectrometry 2009-07, Vol.20 (7), p.1349-1354
Main Authors: Crizer, David M., McLuckey, Scott A.
Format: Article
Language:English
Subjects:
Alkylation
Amides - chemistry
Aminoacids, peptides. Hormones. Neuropeptides
Analytical Chemistry
Analytical, structural and metabolic biochemistry
Azo Compounds - chemistry
Bioinformatics
Biological and medical sciences
Biotechnology
Bonding strength
Cations
Cations - chemistry
Channels
Chemistry
Chemistry and Materials Science
Electron transfer
Electrons
Fundamental and applied biological sciences. Psychology
Hydrogen Bonding
Mass spectrometry
Methylation
Models, Molecular
Nitrogen
Nitrogen - chemistry
Organic Chemistry
Peptides
Peptides - chemistry
Proteins
Proteomics
Reaction products
Short Communication
Tandem Mass Spectrometry - methods
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Summary:Unmodified and amide nitrogen methylated peptide cations were reacted with azobenzene radical anions to study the utility of electron transfer dissociation (ETD) in analyzing N-methylated peptides. We show that methylation of the amide nitrogen has no deleterious effects on the ETD process. As a result, location of alkylation on amide nitrogens should be straightforward. Such a modification might be expected to affect the ETD process if hydrogen bonding involving the amide hydrogen is important for the ETD mechanism. The partitioning of the ion/ion reaction products into all of the various reaction channels was determined and compared for modified and unmodified peptide cations. While subtle differences in the relative abundances of the various ETD channels were observed, there is no strong evidence that hydrogen bonding involving the amide nitrogen plays an important role in the ETD process. ETD can readily indicate N-methylated peptides. Modified and unmodified forms undergo very similar dissociation.
ISSN:1044-0305
1879-1123
DOI:10.1016/j.jasms.2009.03.023