Protein glycation is a disease associated, non-enzymatic, posttranslational modification generated by endogenous dicarbonyl metabolites. One example from this class of compounds is methylglyoxal (MGO). MGO is a carbohydrate-derived metabolite naturally produced in living cells. MGO is electrophilic and can form covalent adducts with proteins, which in turn influences cell signaling. Consequently, MGO is implicated in numerous diseases such as cancer, neurodegeneration, diabetes, and cardiovascular disease. Existing chemical tools to investigate MGO and MGO modified proteins are limited, leading to an incomplete understanding of its physiological and disease-causing roles. Here, we report a chemical biology platform, termed T-DiP (targetable-dicarbonyl precursor), that releases a physiologically relevant dose of bio-orthogonally functionalized dicarbonyl probe upon irradiation with 365 nm light. This approach, coupled with bio-orthogonal chemistry, enables protein glycation to be controlled and detected with spatiotemporal precision within live cells. This work expands the chemical toolbox needed to elucidate the roles of glycated proteins across various pathologies.

Controlling protein glycation with spatiotemporal control

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ACS Fall 2022

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