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Remodelin, a potential inhibitor for premature aging disease, shows protein reactivity and assay interference. It does not specifically inhibit RNA acetyltransferase NAT10 or its RNA acetylation activity.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Chemical Biology

Background:

  • Remodelin is investigated as a small molecule inhibitor of RNA acetyltransferase NAT10.
  • NAT10 is implicated in Hutchinson-Gilford Progeria Syndrome (HGPS), a premature aging disease.

Purpose of the Study:

  • To evaluate remodelin's assay interference properties.
  • To assess remodelin's effects on NAT10-catalyzed RNA cytidine acetylation.

Main Methods:

  • Assay interference testing (ALARM NMR, proteome-wide affinity profiling).
  • Biophysical analyses (e.g., to assess binding to NAT10 active site).
  • Cellular studies to analyze N4-acetylcytidine (ac4C) modification.

Main Results:

  • Remodelin exhibits cryptic assay interference and protein reactivity.
  • No direct interaction between remodelin and the NAT10 active site was observed.
  • Remodelin treatment did not affect NAT10-dependent ac4C RNA modification in cells.

Conclusions:

  • Remodelin's chemotype may interact with multiple protein targets.
  • Remodelin is not a specific chemical inhibitor of NAT10-catalyzed RNA acetylation.
  • Caution is advised when using remodelin as a specific NAT10 inhibitor in research.