Some biotechnology companies are developing chaperone proteins as a treatment for certain disorders. Name a disease that a chaperone protein might be able to treat, and suggest how it would do so.

Many of the neurodegenerative disorders are the result of the flaws in the folding of the protein, which comprises Parkinson, Alzheimer, prion, and Huntington diseases. Once the protein specific to disease misfolds, it can then produce toxic masses that gather in the brain, resulting in cell death, neuronal dysfunction, and clinical symptoms.

As misfolding of proteins and the gathering of masses are the most upstream occurrences in the pathological cascade, thus, stabilizing or rescuing the native conformations of proteins is a better therapeutic approach.

In the present times, small molecules called chaperones have been demonstrated to be effective in minimizing the levels of misfolded proteins, thus reducing the gathering of masses and their downstream pathological outcomes. Chaperones are categorized as pharmacological, molecular, or chemical.