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Prion diseases are invariably fatal neurodegenerative diseases that affecthumans and animals. Unlike most other amyloid forming neurodegenerativediseases, these can be highly infectious. Prion diseases occur in a variety ofspecies. They include the fatal human neurodegenerative diseasesCreutzfeldt-Jakob Disease (CJD), Fatal Familial Insomnia (FFI),Gerstmann-Straussler-Scheinker syndrome (GSS), Kuru, the bovine spongiformencephalopathy (BSE or 'mad-cow' disease) in cattle, the chronic wastingdisease (CWD) in deer and elk, and scrapie in sheep and goats, etc.Transmission across the species barrier to humans, especially in the case ofBSE in Europe, CWD in North America, and variant CJDs (vCJDs) in young peopleof UK, is a major public health concern. Fortunately, scientists reported thatthe (central) hydrophobic region of prion proteins (PrP) controls the formationof diseased prions. This article gives a detailed survey on PrP hydrophobicregion and does molecular dynamics studies of human PrP(110-136) to confirmsome findings from the survey. The structural bioinformatics presented in thisarticle can be helpful as a reference in three-dimensional images forlaboratory experimental works to study PrP hydrophobic region.

A survey and a molecular dynamics study on the (central) hydrophobic region of prion proteins