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Photocaged dicarbonyl probe provides spatiotemporal control over protein glycation.

ABSTRACT: Protein glycation is a disease associated, non-enzymatic, posttranslational modification generated by endogenous dicarbonyl metabolites. Currently, there is a lack of chemical tools capable of studying protein adducts caused by this class of reactive species. 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 enables protein glycation to be controlled with spatiotemporal precision within live cells and expands the chemical toolbox needed to elucidate the roles of glycated proteins across various pathologies.

SUBMITTER: Hurben AK

PROVIDER: S-EPMC10620854 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature

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Photocaged dicarbonyl probe provides spatiotemporal control over protein glycation.

Hurben Alexander K AK Ge Peng P Bouchard Jacob L JL Doran Todd M TM Tretyakova Natalia Y NY

Chemical communications (Cambridge, England) 20220118 6

Protein glycation is a disease associated, non-enzymatic, posttranslational modification generated by endogenous dicarbonyl metabolites. Currently, there is a lack of chemical tools capable of studying protein adducts caused by this class of reactive species. 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 ...[more]

PMID: 34935009

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