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Exploring Protein Structure and Interactions via Electrophoto-XL-MS with Phosphate-Enrichable Cross-linker

ABSTRACT: Chemical cross-linking mass spectrometry (XL-MS) is a powerful research tool for exploring protein-protein interactions and their three-dimensional structures. To further increase cross-link coverage, a novel, methyurazole-derived, enrichable trifunctional cross-linker—phospho bismethylurazole (pBMT) was developed. The phosphate group, a small affinity tag, successfully separates cross-linked peptides from high-abundance noncross-linked peptides. The cross-linking strategy was developed to target multiple amino acid types ( i.e., tyrosine and histidine) under electrochemical and photochemical conditions without additional side reactions. This method was applied to cross-linking peptides, proteins, protein complexes, and cell lysates. Analysis of cross-linking results indicates that the pBMT-based cross-linking strategy provides abundant and accurate information for facilitating protein structure elucidation. Altogether, pBMT provides a novel chemical biology tool and innovative thought for the in-depth exploration of dynamic interactions between proteins

ORGANISM(S): Homo Sapiens Mus Musculus

SUBMITTER: Zhonglin Wei

PROVIDER: PXD082104 | iProX | Mon Aug 03 00:00:00 GMT+01:00 2026

REPOSITORIES: iProX

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