Self-reporting fluorescent substrates of protein tyrosine kinases

Qunzhao Wang, Sean M. Cahill, Michael Blumenstein, David S. Lawrence

Research output: Contribution to journalArticle

63 Citations (Scopus)

Abstract

A new mechanistic principle by which protein tyrosine kinase substrates fluorescently report the introduction of a phosphate moiety has been developed. NMR was used to establish that tyrosine phosphorylation induces the disruption of π-π stacking interactions of the tyrosine moiety with a proximal fluorophore on the peptide substrate. We have demonstrated that (1) the peptide substrates described in this study are useful for a wide variety of different tyrosine kinases, (2) physiological concentrations of ATP can be employed (unlike the standard radioactive ATP kinase assays), thus providing a more realistic assessment of inhibitor potency, and (3) protein kinase self-activation can be observed in real-time.

Original languageEnglish (US)
Pages (from-to)1808-1809
Number of pages2
JournalJournal of the American Chemical Society
Volume128
Issue number6
DOIs
StatePublished - Feb 15 2006

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Protein-Tyrosine Kinases
Tyrosine
Adenosine Triphosphate
Adenosinetriphosphate
TYK2 Kinase
Proteins
Peptides
Substrates
Protein Kinases
Phosphorylation
Phosphotransferases
Fluorophores
Phosphates
Assays
Chemical activation
Nuclear magnetic resonance

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Self-reporting fluorescent substrates of protein tyrosine kinases. / Wang, Qunzhao; Cahill, Sean M.; Blumenstein, Michael; Lawrence, David S.

In: Journal of the American Chemical Society, Vol. 128, No. 6, 15.02.2006, p. 1808-1809.

Research output: Contribution to journalArticle

Wang, Qunzhao ; Cahill, Sean M. ; Blumenstein, Michael ; Lawrence, David S. / Self-reporting fluorescent substrates of protein tyrosine kinases. In: Journal of the American Chemical Society. 2006 ; Vol. 128, No. 6. pp. 1808-1809.
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