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  • Title: Selection of inhibitory peptides for Aurora-A kinase from a phage-displayed library of helix-loop-helix peptides.
    Author: Fujiwara D, Ye Z, Gouda M, Yokota K, Tsumuraya T, Fujii I.
    Journal: Bioorg Med Chem Lett; 2010 Mar 01; 20(5):1776-8. PubMed ID: 20117931.
    Abstract:
    Conformationally constrained peptide libraries have been made by grafting randomized amino acid sequences onto a rigid scaffold derived from natural proteins. Here, as a library scaffold, we propose a de novo designed helix-loop-helix motif. We constructed a peptide library of the loop region and screened against Aurora-A, which is a member of the Aurora family of serine/threonine protein kinases, to successfully isolate the inhibitory peptides. A semi-rational strategy, which combines phage-displayed libraries and de novo designed peptides, would provide a new way to generate selective peptide inhibitors for the protein kinase family.
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