Why prions are so hard to destroy

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Nearly all organic material (like bacteria and viruses) is destroyed at temperatures above 60° Celsius. Some temperature resistant pathogens can survive slightly higher temperatures than this, but even the most hardy will be destroyed at temperatures above 150° Celsius.

But for prions these temperatures are hardly sufficient. They can survive being frozen, cooked, steamed, and even chemically treated with substances like formaldehyde and alcohol. Temperatures as high as 600° Celsius will not reliably kill them, and only in the 1000° Celsius range are they destroyed. At this temperatures, most *metals* will melt.

Why are prions so hard to destroy if they are chemically identical to the organic material inside our body already?

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Anonymous 0 Comments

A bit more specifics on prions.

Proteins, which they are made of, tend to denature at higher temperatures. They are folded in a specific way, and if you imagine temperature as other atoms bumping into the protein, the hotter it is the faster the bump meaning at some point it overcomes the folds and forces it into positions it doesn’t naturally fold into which is essential for its operation.

Cooling it down doesn’t necessarily mean it will fold the right way, it may actually misfold and be rendered inoperable and this is probably what happens most of the time. But some of the prions will refold back into their prion shape. And that will be enough to infect someone.

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