Atomic-resolution structures of prion AGAAAAGA amyloid fibrils

Details Atomic-resolution structures of prion AGAAAAGA amyloid fibrils Atomic-resolution structures of prion AGAAAAGA amyloid fibrils

2011-06-09

arxiv.org/abs/1106.1721v1

Physics

Biological Physics

book Chapter of Amyloids: Composition, Functions and Pathology, NOVA Publishers, 2011

Scientific paper

To the best of the author's knowledge, there is little structural data available on the AGAAAAGA palindrome in the hydrophobic region (113-120) of prion proteins due to the unstable, noncrystalline and insoluble nature of the amyloid fibril, although many experimental studies have shown that this region has amyloid fibril forming properties and plays an important role in prion diseases. In view of this, the present study is devoted to address this problem from computational approaches such as local optimization steepest descent, conjugate gradient, discrete gradient and Newton methods, global optimization simulated annealing and genetic algorithms, canonical dual optimization theory, and structural bioinformatics. The optimal atomic-resolution structures of prion AGAAAAGA amyloid fibils reported in this Chapter have a value to the scientific community in its drive to find treatments for prion diseases or at least be useful for the goals of medicinal chemistry.

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