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  • Title: Phosphopeptides with improved cellular uptake properties as ligands for the polo-box domain of polo-like kinase 1.
    Author: Richter S, Neundorf I, Loebner K, Gräber M, Berg T, Bergmann R, Steinbach J, Pietzsch J, Wuest F.
    Journal: Bioorg Med Chem Lett; 2011 Aug 15; 21(16):4686-9. PubMed ID: 21778054.
    Abstract:
    Human polo-like kinase 1 (Plk1) is involved in cell proliferation and overexpressed in a broad variety of different cancer types. Due to its crucial role in cancerogenesis Plk1 is a potential target for diagnostic and therapeutic applications. Peptidic ligands can specifically interact with the polo-box domain (PBD) of Plk1, a C-terminal located phosphoepitope binding motif. Recently, phosphopeptide MQSpTPL has been identified as ligand with high binding affinity. However, a radiolabeled version of this peptide showed only insufficient cellular uptake. The present study investigated peptide dimers consisting of PBD-targeting phosphopeptide MQSpTPL and a cell-penetrating peptide (CPP) moiety. The new constructs demonstrate superior uptake in different cancer cell-lines compared to the phosphopeptide alone. Furthermore, we could demonstrate binding of phosphopeptide-CPP dimers to PBD of Plk1 making the compounds interesting leads for the development of molecular probes for imaging Plk1 in cancer.
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