Structure-activity relationship of a novel peptide substrate for p60c-src protein tyrosine kinase

Qiang Lou, Jinzi Wu, Sydney E. Salmon, Kit Lam

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


We recently reported the identification of a peptide (YIYGSFK) as an efficient substrate for p60c-src using a random combinatorial peptide library screening method. Over 70 analogues of YIYGSFK were designed and synthesized on beads and their phosphorylation on solid phase by p60c-src was quantitated by the PhosphorImager. A hydrophobic l-amino acid in position 2 and a basic amino acid in position 7 proved crucial for activity as a substrate. In addition, the l-tyrosine residue at position 3 was critical as the phosphorylation site and was found to be stereospecific, as substitution with the d-enantiomer at this position rendered the peptide totally inactive.

Original languageEnglish (US)
Pages (from-to)289-296
Number of pages8
JournalLetters in Peptide Science
Issue number5
StatePublished - Jan 1996
Externally publishedYes


  • Combinatorial libraries
  • p60
  • Peptide substrate
  • Protein tyrosine kinases

ASJC Scopus subject areas

  • Biochemistry


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