Prion diseases are caused by the conformational change of cellular prion protein PrPC into pathological prion protein PrPSc. Here we study the effect of zinc on the aggregation and conformational change of human prion protein (PrP). As revealed by thioflavin T binding assays, Sarkosyl-soluble SDS-PAGE, and transmission electron microscopy, aggregation of wild-type PrP in the absence of Zn2+ undergoes four steps: amorphous aggregates, profibrils, mature fibrils, and fragmented fibrils. http://www.ncbi.nlm.nih.gov/pubmed/25922234 Courtesy: Pan et al., 2015

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