Deep Structural Characterization of Protein-Bound Lipids via Native MS and Ultraviolet Photodissociation.

ABSTRACT: Protein-lipid interactions are critical for maintaining membrane protein structure and regulating diverse protein functions. Native mass spectrometry (MS) has emerged as a powerful technique for the direct observation and characterization of protein-lipid complexes. However, intact mass measurements alone cannot resolve important structural details such as the identity of lipid acyl chains and their modifications. To fully characterize protein-bound lipids, we present a multistage native MS method that leverages ultraviolet photodissociation to elucidate the precise molecular composition of heterogeneous protein-lipid assemblies. We demonstrate the utility of this approach for both soluble and membrane proteins. First, we comprehensively define the endogenous lipids bound to the bacterial

SUBMITTER: Kirschbaum C 

PROVIDER: S-EPMC12424025 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature