Letters in Peptide Science

, Volume 6, Issue 5–6, pp 335–341 | Cite as

p56lck SH2 domain binding motifs from bead binding screening of peptide libraries containing phosphotyrosine surrogates

Article

Summary

Phosphorylation reactions are key meditors in a variety of biochemical signal processes. Research into the selective inhibition of protein tyrosine kinases to generate anticancer agents has madeO-phosphotyrosyl analogues important pharmacological tools. The simple procedures reported here involving the formation of interative peptide libraries together with the development of a selective and sensitive bead-binding assay have made it possible to rapidly screen peptides incorporatingO-phosphotyrosyl surrogates (includingO-phospho-2,3,5,6-tetrafluorotyrosine, 4-(phosphono)hydroxymethyl-phenylalanine and 4-(phosphono)fluoromethyl-phenylalanine) for their potential to inhibit the protein tyrosine kinase p56lck. These procedures can be easily adapted to combinatorical peptide libraries.

Key words

peptide libraries phosphotyrosine analogues protein tyrosine kinases p56lck 

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Copyright information

© Kluwer Academic Publishers 1999

Authors and Affiliations

  1. 1.Division of Biochemitry and Molecular Biology, School of Biological SciencesUniversity of SouthamptonSouthamptonU.K.

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