Development of stable phosphohistidine analogues

Jung Min Kee, Bryeanna Villani, Laura R. Carpenter, Tom W. Muir

Research output: Contribution to journalArticle

100 Scopus citations

Abstract

Protein phosphorylation is one of the most common and extensively studied posttranslational modifications (PTMs). Compared to the O-phosphorylation of Ser, Thr, and Tyr residues, our understanding of histidine phosphorylation is relatively limited, particularly in higher eukaryotes, due to technical difficulties stemming from the intrinsic instability and isomerism of phosphohistidine (pHis). We report the design and synthesis of stable and nonisomerizable pHis analogues. These pHis analogues were successfully utilized in solid-phase peptide synthesis and semi-synthesis of histone H4. Significantly, the first antibody that specifically recognizes pHis was obtained using the synthetic peptide as the immunogen.

Original languageEnglish (US)
Pages (from-to)14327-14329
Number of pages3
JournalJournal of the American Chemical Society
Volume132
Issue number41
DOIs
StatePublished - Oct 20 2010

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Fingerprint Dive into the research topics of 'Development of stable phosphohistidine analogues'. Together they form a unique fingerprint.

  • Cite this