Abstract
We investigated the interaction between Polo-Box Domain (PBD) of polo-like kinase 1 (Plk1) and Bora peptide based on protein-protein interactions using the Proteochip (Proteogen, Korea) technology. Plk-1 protein conjugated with GST was bound to anti-GST antibody immobilized on the surface of the Proteochip, after which a Bora peptide labeled with a fluorescent dye, Cy5, was interacted with the Plk-1 protein on the chip in a dose-dependent manner. A chemical compound E8 was screened as a novel inhibitor against the Plk1-Bora interaction using the Proteochip. The compound significantly inhibited NCI-H460 (lung cancer) cell proliferation in vitro in a dose-dependent manner. The protein chip-based Plk1-Bora binding system will serve a novel promising tool which is applicable for screening of novel inhibitors against Plk1, regardless of the enzyme activity.
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Lee, Jk., Kang, IC. Analysis of Plk1-Bora interaction using a protein chip system. BioChip J 7, 151–155 (2013). https://doi.org/10.1007/s13206-013-7208-6
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DOI: https://doi.org/10.1007/s13206-013-7208-6