Tight-binding inhibitory sequences against pp60c−srcidentified using a random 15-amino-acid peptide library
- 2 December 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 399 (3) , 237-240
- https://doi.org/10.1016/s0014-5793(96)01329-4
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 μM, whereas replacing the glycines with proline increased the K i value to 3.1 mM.Keywords
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