Proteomics

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Retention-Modulating Derivatization Unlocks Full Structural Resolution of Glycerophospholipid Isomers


ABSTRACT: The precise structural characterization of lipids is fundamental to understanding their biological roles. However, full structural resolution of complex lipids at the isomer level remains a significant challenge. Here, we propose an integrated orthogonal analysis strategy that simultaneously resolves lipid C=C bond location, C=C bond configuration, and sn-position in a single injection, enabling complete structural elucidation of glycerophospholipids at the isomer level. This method is based on the principles of simultaneous C=C bond activation and fatty acyl chain polarity difference modulation. By introducing a specific N-benzyl-aziridine structure at the double bond of fatty acyl chains, this derivatization enables C=C bond location identification based on induced characteristic fragmentation, C=C bond configuration assignment based on specific chromatographic elution order, and sn-position identification based on amplified chromatographic separation and characteristic fragmentation. Using the established

ORGANISM(S): Acyrthosiphon Pisum

SUBMITTER: Suming Chen  

PROVIDER: PXD074228 | iProX | Sat Feb 07 00:00:00 GMT 2026

REPOSITORIES: iProX

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