Positional effects of monofluorinated phenylalanines on histone acetyltransferase stability and activity

Natalya Voloshchuk, Anita Y. Zhu, David Snydacker, Jin Kim Montclare

Research output: Contribution to journalArticle


To explore the impact of global incorporation of fluorinated aromatic amino acids on protein function, we investigated the effects of three monofluorinated phenylalanine analogs para-fluorophenylalanine (pFF), meta-fluorophenylalanine (mFF), and ortho-fluorophenylalanine (oFF) on the stability and enzymatic activity of the histone acetyltransferase (HAT), tGCN5. We selected this set of fluorinated amino acids because they bear the same size and overall polarity but alter in side chain shape and dipole direction. Our experiments showed that among three fluorinated amino acids, the global incorporation of pFF affords the smallest perturbation to the structure and function of tGCN5.

Original languageEnglish (US)
Pages (from-to)5449-5451
Number of pages3
JournalBioorganic and Medicinal Chemistry Letters
Issue number18
StatePublished - Sep 15 2009



  • Activity
  • Fluorinated amino acids
  • Histone acetyltransferase
  • Protein design
  • Stability

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

Cite this