Review Molecular dynamics studies on 3D structures of the hydrophobic region PrP(109-136)

Prion diseases, traditionally referred to as transmissible spongiform encephalopathies, are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species, manifesting as scrapie in sheep, bovine spongiform encephalopathy (or ‘mad-cow ’ disease) in cattle, and Creutzfeldt–Jakob disease, Gerstmann–Strussler–Scheinker syndrome, fatal familial insomnia (FFI), and Kulu in humans, etc. These neurode-generative diseases are caused by the conversion from a soluble normal cellular prion protein (PrPC) into insoluble abnormally folded infectious prions (PrPSc). The hydro-phobic region PrP(109-136) controls the formation of dis-eased prions: the normal PrP(113-120) AGAAAAGA palindrome is an inhibitor/blocker of prion diseases and the highly conserved glycine-xxx-glycine motif PrP(119-131) can inhibit the formation of infectious prion proteins in cells. This article gives detailed reviews on the PrP(109-136) region and presents the studies of its three-dimen-sional structures and structural dynamics