Revealing deamidation and isoaspartate formation during peptide analysis, purification and storage by tandem mass spectrometry.

ABSTRACT: Interest in peptides and peptidomimetics continues to grow, particularly in the context of drug discovery and development. However, spontaneous chemical modifications such as deamidation and isoaspartate formation present significant challenges, as they are difficult to detect and can compromise peptide integrity and function. Conventional chromatographic methods and standard mass spectrometric analyses often fail to distinguish structurally similar peptides with nearly identical physicochemical properties and masses. In this study, tandem mass spectrometry (MS/MS) was employed to monitor deamidation events involving asparagine, glutamine and C-terminal amide functional groups. Both collision-induced dissociation (CID) and electron-transfer dissociation (ETD) were systematically evaluated

SUBMITTER: Erckes V 

PROVIDER: S-EPMC12801052 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature