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

✍ Scribed by Qiang Lou; Jinzi Wu; Sydney E. Salmon; Kit S. Lam

Book ID
104639615
Publisher
Springer Netherlands
Year
1996
Tongue
English
Weight
666 KB
Volume
2
Category
Article
ISSN
1573-3149

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✦ Synopsis

We recently reported the identification of a peptide (YIYGSFK) as an efficient substrate for p60 c-s~c 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 p60 csrc 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.

📜 SIMILAR VOLUMES

Identification of GIYWHHY as a novel pep
Identification of GIYWHHY as a novel peptide substrate for human p60c-src protein tyrosine kinase
✍ Qiang Lou; Margaret E. Leftwich; Kit S. Lam 📂 Article 📅 1996 🏛 Elsevier Science 🌐 English ⚖ 600 KB

We have recently determined that -Ile-Tyr- were the two critical residues as a peptide substrate for p60c-src protein tyrosine kinase (Lou, Q. et al., Lett. Peptide Sci., 1995, 2, 289). Here, we report on the design and synthesis of a secondary 'one-bead, one-compound' combinatorial peptide library