Potent inhibition of protein-tyrosine phosphatase-1B using the phosphotyrosyl mimetic fluoro-O-malonyl tyrosine (FOMT)

Peter P. Roller, Li Wu, Zhong Yin Zhang, Terrence R. Burke

Research output: Contribution to journalArticle

28 Scopus citations


To enhance PTP binding interactions, both inside and outside the pTyr binding pocket, a thioether-cyclized peptide has been designed based on the EGF receptor autophosphorylation sequence (EGFR988-993) 'Asp-Ala-Asp- Glu-pTyr-Leu', in which the pTyr residue has been replaced by the nonphosphorus-containing pTyr mimetic fluoro-O-malonyltyrosine (FOMT, 2). The resulting peptide 4 exhibits a K(i) value of 170 nM, making it one of the most potent inhibitors of PTP1B yet reported.

Original languageEnglish (US)
Pages (from-to)2149-2150
Number of pages2
JournalBioorganic and Medicinal Chemistry Letters
Issue number16
StatePublished - Aug 18 1998


ASJC Scopus subject areas

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

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