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- Development of cyclic peptomer inhibitors targeting the polo-box domain of polo-like kinase 1
- R N Murugan; J E Park; D Lim; M Ahn; C Cheong; Taeho Kwon; K Y Nam; S H Choi; Bo Yeon Kim; D Y Yoon; M B Yaffe; Dae Yeul Yu; K S Lee; J K Bang
- Bibliographic Citation
- Bioorganic & Medicinal Chemistry, vol. 21, no. 9, pp. 2623-2634
- Publication Year
- The polo-box domain (PBD) of polo-like kinase 1 (Plk1) is essentially required for the function of Plk1 in cell proliferation. The availability of the phosphopeptide-binding pocket on PBD provides a unique opportunity to develop novel protein-protein interaction inhibitors. Recent identification of a minimal 5-residue-long phosphopeptide, PLHSpT, as a Plk1 PBD-specific ligand has led to the development of several peptide-based inhibitors, but none of them is cyclic peptide. Through the combination of single-peptoid mimics and thio-ether bridged cyclization, we successfully demonstrated for the first time two cyclic peptomers, PL-116 and PL-120, dramatically improved the binding affinity without losing mono-specificity against Plk1 PBD in comparison with the linear parental peptide, PLHSpT. These cyclic peptomers could serve as promising templates for future drug designs to inhibit Plk1 PBD.
- Cyclic peptomersKinase inhibitorsPolo-box domain (PBD)Solid phase peptide synthesis
- Appears in Collections:
- Jeonbuk Branch Institute > Primate Resources Center > 1. Journal Articles
Ochang Branch Institute > Chemical Biology Research Center > 1. Journal Articles
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