Application

DHSO Crosslinker is a homobifunctional, acidic residue-targeting, sulfoxide-containing crosslinker for analysis of protein-protein interactions (PPIs) through crosslinking mass spectrometry (XL-MS). DHSO possesses two hydrazide-reactive groups for targeting aspartic acid (Asp) and glutamic acid (Glu) and two symmetrical C-S cleavable bonds adjacent to the central sulfoxide. While former amine-reactive reagents react with lysine (Lys) residues in proximity to the PPI, targeting acidic residues provides further opportunity to characterize protein interaction surfaces at which Asp and Glu are often prevalent. Additionally, the 12.4 Å spacer yields tagged peptides post-cleavage for unambiguous identification by collision-induced dissociation in tandem MS. DHSO Crosslinker provides complementary data to Lys-targeting reagents and will find wide utility in the elucidation of PPIs, study of proteins that function as complexes, quantification of structural dynamics, and quest for targeting "undruggable" protein targets.

Legal Information

Subject to US Patent Application #15/613,065 of the Regents of the University of California

Other Notes

Technology Spotlight: Cross-Linkers for Elucidation of Protein-Protein InteractionsDeveloping an Acidic Residue Reactive and Sulfoxide-Containing MS-Cleavable Homobifunctional Cross-Linker for Probing Protein–Protein InteractionsDevelopment of a Novel Sulfoxide-Containing MS-Cleavable Homobifunctional Cysteine-Reactive Cross-Linker for Studying Protein–Protein InteractionsStructural dynamics of the human COP9 signalosome revealed by cross-linking mass spectrometry and integrative modeling