3,3′-Sulfinylbis(N-(2-(2,5-dioxo-2,5-dihydro-1H-pyrrol-1-yl)ethyl)propanamide), Mass spectrometry-cleavable crosslinker for studying protein-protein interations
BMSO (bismaleimide sulfoxide) crosslinker is a homobifunctional, cysteine residue-targeting, sulfoxide-containing crosslinker for analysis of protein-protein interactions (PPIs) through crosslinking mass spectrometry (XL-MS). BMSO possesses two maleimide reactive groups for targeting Cys, a 24.2 Å spacer arm, and two symmetrical C-S cleavable bonds adjacent to the central sulfoxide. While similar reagents react with lysine (Lys) and acidic residues, targeting Cys provides further opportunity to characterize protein interaction surfaces. Additionally, the post-cleavage spacer yields tagged peptides for unambiguous identification by collision-induced dissociation in tandem MS.
BMSO crosslinker provides complementary data to amine-reactive and acidic residue-targeting reagents and will find wide utility in the elucidation of PPIs, study of proteins that function as complexes, quantification of structural dynamics, and the quest for targeting "undruggable" protein targets.
Cross-linking mass spectrometry (XL-MS) has become an emerging technology for defining protein-protein interactions (PPIs) and elucidating architectures of large protein complexes. Up to now, the most widely used cross-linking reagents target lysines. Although such reagents have been successfully applied to
Proceedings of the National Academy of Sciences of the United States of America, 117(8), 4088-4098 (2020-02-09)
The COP9 signalosome (CSN) is an evolutionarily conserved eight-subunit (CSN1-8) protein complex that controls protein ubiquitination by deneddylating Cullin-RING E3 ligases (CRLs). The activation and function of CSN hinges on its structural dynamics, which has been challenging to decipher by