  Many experimental studies have shown that the prion AGAAAAGA palindrome
hydrophobic region (113-120) has amyloid fibril forming properties and plays an
important role in prion diseases. However, due to the unstable, noncrystalline
and insoluble nature of the amyloid fibril, to date structural information on
AGAAAAGA region (113-120) has been very limited. This region falls just within
the N-terminal unstructured region PrP (1-123) of prion proteins. Traditional
X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy
experimental methods cannot be used to get its structural information. Under
this background, this paper introduces a novel approach of the canonical dual
theory to address the 3D atomic-resolution structure of prion AGAAAAGA amyloid
fibrils. The novel and powerful canonical dual computational approach
introduced in this paper is for the molecular modeling of prion AGAAAAGA
amyloid fibrils, and that the optimal atomic-resolution structures of prion
AGAAAAGA amyloid fibils presented in this paper are useful for the drive to
find treatments for prion diseases in the field of medicinal chemistry.
Overall, this paper presents an important method and provides useful
information for treatments of prion diseases. Overall, this paper could be of
interest to the general readership of Theoretical Biology.
