TAILIEUCHUNG - Báo cáo khoa hoc : The prion protein binds thiamine

Although highly conserved throughout evolution, the exact biological function of the prion protein is still unclear. In an effort to identify the potential biological functions of the prion protein we conducted a small-molecule screening assay using the Syrian hamster prion protein [shPrP(90– 232)]. | IFEBS Journal The prion protein binds thiamine Rolando Perez-Pineiro1 Trent C. Bjorndahl1 Mark V. Berjanskii2 David Hau1 Li Li3 Alan Huang3 Rose Lee3 Ebrima Gibbs3 Carol Ladner1 Ying Wei Dong1 Ashenafi Abera1 Neil R. Cashman3 and David S. Wishart1 2 1 Department of BiologicalSciences University of Alberta Edmonton AB Canada 2 Department of Computing Science University of Alberta Edmonton AB Canada 3 Brain Research Centre University of British Columbia Vancouver BC Canada Keywords binding in silico docking NMR screening prion protein thiamine Correspondence D. S. Wishart Departments of Biological Sciences and Computing Science University of Alberta Rm. 2-21 Athabasca Hall University of Alberta Edmonton AB Canada T6G 2E8 Fax 1 780 492 1071 Tel 1 780 492 0383 E-mail These authors contributed equally to this study Received 20 March 2011 revised 7 August 2011 accepted 11 August 2011 doi Although highly conserved throughout evolution the exact biological function of the prion protein is still unclear. In an effort to identify the potential biological functions of the prion protein we conducted a smallmolecule screening assay using the Syrian hamster prion protein shPrP 90-232 . The screen was performed using a library of 149 water-soluble metabolites that are known to pass through the blood-brain barrier. Using a combination of 1D NMR fluorescence quenching and surface plasmon resonance we identified thiamine vitamin B1 as a specific prion ligand with a binding constant of 60 IM. Subsequent studies showed that this interaction is evolutionarily conserved with similar binding constants being seen for mouse hamster and human prions. Various protein construct lengths both with and without the unstructured N-terminal region in the presence and absence of copper were examined. This indicates that the N-terminus has no influence on the protein s ability to interact with thiamine. In addition to thiamine the more .

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