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PreprintCC BY-NC-NDbioRxiv

Chemical proteomics suggests sofosbuvir is metabolically attached to proteins through a UMPylation-like pathway.

  • M. Hertwig
  • P. Kielkowski1
  1. 1LMU Munich, Department of Chemistry
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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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Cite

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BibTeX
@misc{hertwig2026chemical,
  title = {{Chemical proteomics suggests sofosbuvir is metabolically attached to proteins through a UMPylation-like pathway.}},
  author = {M. Hertwig and P. Kielkowski},
  howpublished = {bioRxiv},
  year = {2026},
  month = oct,
  doi = {10.64898/2026.10.17.759838},
  url = {https://www.biorxiv.org/content/10.64898/2026.10.17.759838v1},
  note = {CC BY-NC-ND},
}
RIS
TY  - UNPB
TI  - Chemical proteomics suggests sofosbuvir is metabolically attached to proteins through a UMPylation-like pathway.
AU  - M. Hertwig
AU  - P. Kielkowski
PY  - 2026
DA  - 2026/10/17
PB  - bioRxiv
DO  - 10.64898/2026.10.17.759838
UR  - https://www.biorxiv.org/content/10.64898/2026.10.17.759838v1
AB  - 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.
ER  -