Tight-binding inhibitory sequences against pp60(c-src) identified using a random 15-amino-acid peptide library

Toru Nishi, Raymond J.A. Budde, John S. McMurray, Nihal U. Obeyesekere, Naueen Safdar, Victor A. Levin, Hideyuki Saya

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

A bacteriophage peptide library containing a random 15-amino-acid insert was screened for identification of peptide sequence(s) that bind pp60(c-src). Sequencing the random insert from more than 100 virions indicated that more than 60% of the phage virions that bound to this enzyme contained a GXXG sequence motif in which X was frequently a hydrophobic residue. The GXXG sequence was often repeated as GXXGXXG. Two nonameric peptides were synthesized to determine whether or not the peptide inhibits pp60(c-src) tyrosine kinase activity and the importance of the glycine residues within this sequence. The peptide containing glycine had a K(i) of 24 μM, whereas replacing the glycines with proline increased the K(i) value to 3.1 mM.

Original languageEnglish
Pages (from-to)237-240
Number of pages4
JournalFEBS Letters
Volume399
Issue number3
DOIs
Publication statusPublished - 16-12-1996
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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