RT Dissertation/Thesis
T1 Structural characterization of recombinant PrPSc prions using biochemical and biophysical techniques
A1 Bugallo Codeseira, Yaiza
K1 Prion
K1 NMR
K1 protein
K1 structure
AB Prion diseases i.e. Creutzfeldt-Jakob disease (CJD) and related disorders,are rare, fatal brain neurodegenerative ailments. Their worldwide yearly incidence is of about one case per millionpeople, i.e., approximately 8000 new cases per year in the world. They are caused by the autopropagativemisfolding of the prion protein, PrP, namely PrPSc. Despite extensive efforts, effective drugs against thesedisorders are still lacking, very likely due to the fact that the structure of PrPSc is still unknown.This thesis proposalaims at elucidating the structure of such prion using different biochemical and biophysical techniques. The maintechnique employed is solid state nuclear magnetic resonance (ssNMR) by which we analyzed for the first timerecombinant BVPrPSc sample produced by the PMSA technique, along with some controls that allowed us toobtain an array of structural information. The most relevant piece of information obtained by analyzing 13CO-Phe-Het-s, a yeast prion, 13CO-Phe-PrP amyloid which is non infectious and recBVPrPSc was the secondary structureof the latter conforms to a PIRIBS (parallel-in-register-intermolecular-beta-sheets) structure contrary to our initialhypothesis that its secondary structure was that of a 4RBS (4-rung-beta-solenoid). In my thesis I present all thedetails of how I arrived to this conclusion along with others.
YR 2022
FD 2022
LK http://hdl.handle.net/10347/29264
UL http://hdl.handle.net/10347/29264
LA eng
DS Minerva
RD 28 abr 2026