The prion protein involved in bovine spongiform encephalopathy and variant Creutzfeldt-Jakob disease was dubbed PrP, which, in its normal form, is found in healthy cells.
But when it switches shape to become PrpSc it causes other PrP proteins to follow suit and they go on to form clumps of amyloid, which destroy brain tissue, causing dementia and death.
The current findings "provide a new framework for us to begin exploring properties of prion biology that, up until now, have proven difficult to investigate," Dr. Lindquist said.
The researchers used peptide arrays, usually used to find the active binding sites of well-behaved proteins, to observe prion proteins misfolding and then creating self-perpetuating assemblies of prions.
