Chemical proteomics suggests sofosbuvir is metabolically attached to proteins through a UMPylation-like pathway.
Abstract
Sofosbuvir is a pronucleotide prodrug (ProTide) that releases a uridine monophosphate analogue, which could modify proteins chemically or through UMP-transferring enzymes. Using an alkyne-tagged probe and chemical proteomics, we identified about 120 labelled proteins and a UMPylation-like (+774.31 Da) modification on cathepsin Z, suggesting that nucleotide prodrugs may enter protein nucleotidylation pathways.
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