Untargeted Discovery and Localization of Isomerized Residues in Neuropeptides.

ABSTRACT: A reliable and effective analytical method for discovering and characterizing isomerized residues in physiologically active peptides is essential for their comprehensive characterization. Complete structural detail facilitates the determination of a peptide's biological roles and meets the increasingly stringent demands for peptide-based therapeutics. Here, a comprehensive untargeted analytical workflow predicts possible peptide isomers from peptidomics data and then localizes the isomerized residues by using collision-induced dissociation-trapped ion mobility spectrometry (CID-TIMS) and protein isoaspartyl methyltransferase (PIMT) activity. The approach allows for the discovery and characterization of isomerized isoaspartate (isoAsp) residues and D-amino acids within the peptide. Potentia

SUBMITTER: Okyem S 

PROVIDER: S-EPMC12368835 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature