Prion diseases develop when the normal cellular prion protein (PrPC) undergoes a structural transformation into a misfolded, pathogenic form known as PrPSc. This process involves a change from an alpha-helical structure to a beta-sheet-rich conformation, leading to the formation of insoluble aggregates. These aggregates disrupt cellular functions, causing progressive neurodegeneration and the characteristic spongiform changes in brain tissue. The exact mechanism of this conversion remains a subject of intense research, but it is known that once initiated, it can propagate in a chain reaction, converting more normal proteins into the abnormal form.
