Trioxane-based MS-cleavable cross-linking mass spectrometry for profiling multimeric interactions of cellular networks.

ABSTRACT: Cross-linking mass spectrometry (XL-MS) is a powerful technology for mapping protein-protein interactions (PPIs) at the systems level. While bivalent cross-links are effective for defining protein interactions and structures, multivalent cross-links offer enhanced spatial resolution to facilitate characterization of heterogeneous protein complexes. However, their identification remains challenging due to fragmentation complexity and the vast expansion of database search space. Here, we present tris-succinimidyl trioxane (TSTO), a novel trioxane-based, MS-cleavable homotrifunctional cross-linker capable of targeting three proximal lysines simultaneously. TSTO's unique MS-cleavability enables concurrent release of cross-linked peptide constituents during collision-induced dissociation, permi

SUBMITTER: Yu C 

PROVIDER: S-EPMC12215968 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature