Photocaged dicarbonyl probe provides spatiotemporal control over protein glycation

Alexander K. Hurben; Peng Ge; Jacob L. Bouchard; Todd M Doran; Natalia Y. Tretyakova

doi:10.1039/d1cc06651j

Photocaged dicarbonyl probe provides spatiotemporal control over protein glycation

Alexander K. Hurben, Peng Ge, Jacob L. Bouchard, Todd M Doran, Natalia Y. Tretyakova

Medicinal Chemistry

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3 Scopus citations

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.

Original language	English (US)
Pages (from-to)	855-858
Number of pages	4
Journal	Chemical Communications
Volume	58
Issue number	6
DOIs	https://doi.org/10.1039/d1cc06651j
State	Published - Jan 18 2022

Bibliographical note

Funding Information:
A. K. H. conceptualized this study and wrote the manuscript. Research was performed by A. K. H., P. G., and J. L. B.; T. M. D. and N. Y. T. supervised and provided edits. Microscopy experiments were supported by the University of Minnesota University Imaging Centers (UIC) SCR_020997. This work was funded by the NIH CBITG T32 GM132029 and graciously supported by the UMN Department of Medicinal Chemistry. C. C. Aldrich and S. A. Kennelly provided invaluable edits to this manuscript.

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This journal is © The Royal Society of Chemistry

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title = "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.",

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AU - Bouchard, Jacob L.

AU - Doran, Todd M

AU - Tretyakova, Natalia Y.

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AB - 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.

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Photocaged dicarbonyl probe provides spatiotemporal control over protein glycation

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