Multi-tiered chemical proteomic maps of tryptoline acrylamide-protein interactions in cancer cells.

ABSTRACT: Covalent chemistry is a versatile approach for expanding the ligandability of the human proteome. Activity-based protein profiling (ABPP) can infer the specific residues modified by electrophilic compounds through competition with broadly reactive probes. However, the extent to which such residue-directed platforms fully assess the protein targets of electrophilic compounds in cells remains unclear. Here we evaluate a complementary protein-directed ABPP method that identifies proteins showing stereoselective reactivity with alkynylated, chiral electrophilic compounds-termed stereoprobes. Integration of protein- and cysteine-directed data from cancer cells treated with tryptoline acrylamide stereoprobes revealed generally well-correlated ligandability maps and highlighted features, such as

SUBMITTER: Njomen E 

PROVIDER: S-EPMC11684312 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature