Tight-binding inhibitory sequences against pp60(c-src) identified using a random 15-amino-acid peptide library.
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 Ki of 24 microM, whereas replacing the glycines with proline increased the Ki value to 3.1 mM.
Nishi
T
T
Department of Neuro-Oncology, The University of Texas, M.D. Anderson Cancer Center, Houston 77030, USA.
Budde
R J
RJ
McMurray
J S
JS
Obeyesekere
N U
NU
Safdar
N
N
Levin
V A
VA
Saya
H
H
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D016392:Proto-Oncogene Proteins pp60(c-src) / Q000037:antagonists & inhibitors* / Q000378:metabolism
D010455:Peptides; D016392:Proto-Oncogene Proteins pp60(c-src)