How can prions be killed?

Hint: Prions are misfolded proteins with the capacity to transmit their misfolded form to the same protein's regular variants. In humans and several other species, they describe many lethal and transmissible neurodegenerative illnesses. What causes the normal protein to misfold is not understood, but it is believed that the abnormal three-dimensional structure confers infectious properties.

Complete answer:
Prions form irregular protein aggregates called amyloids. Prions accumulate in contaminated tissue and are associated with damage to the tissue and death of the cells. Several other neurodegenerative disorders, such as Alzheimer's disease and Parkinson's disease, are also responsible for amyloids. Prions are lethal pathogens that are notoriously difficult to inactivate, and there are also insufficient standard microbial disinfection protocols. Extremely simple sodium hypochlorite bleach, sodium hydroxide, and/or extended autoclaving are the recommended remedies for prion decontamination. There are no appropriate prion disease therapies available. There was little improvement in clinical trials in humans and the rarity of prion diseases has hindered them. While some possible therapies have shown promise in the laboratory, once the disease has begun, none has been successful. Also in healthy people and animals, the protein that prions are made of (PrP) is found in the body. PrP, however, has a different structure and is immune to proteases present in infectious material, the enzymes in the body that can usually break down proteins. The protein's normal form is called PrPC.

Therefore, prions are difficult to kill.

Note:
A prion disorder is a type of proteopathy, or structurally abnormal protein disease. Prions also have evidence suggesting that prions may play a role in the Alzheimer's disease process. There have also been some yeast proteins described as having prionogenic properties.