Discrimination of Aspartic and Isoaspartic Acid Residues in Peptides by Tandem Mass Spectrometry with Hydrogen Attachment Dissociation.
Journal
Analytical chemistry
ISSN: 1520-6882
Titre abrégé: Anal Chem
Pays: United States
ID NLM: 0370536
Informations de publication
Date de publication:
13 May 2024
13 May 2024
Historique:
medline:
14
5
2024
pubmed:
14
5
2024
entrez:
14
5
2024
Statut:
aheadofprint
Résumé
Long-lived proteins undergo chemical modifications that can cause age-related diseases. Among these chemical modifications, isomerization is the most difficult to identify. Isomerization often occurs at the aspartic acid (Asp) residues. In this study, we used tandem mass spectrometry equipped with a newly developed ion activation method, hydrogen attachment dissociation (HAD), to analyze peptides containing Asp isomers. Although HAD preferentially produces [c
Identifiants
pubmed: 38741470
doi: 10.1021/acs.analchem.4c00561
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM