Abstract: Amyloid proteins have been known to be responsible for many neurodegenerative diseases of mammals including humans. Histopathologically, amyloids are known to be formed due to misfolds, mutations and other induction events concerned with these proteins in the patients. Once formed, these proteins have been well reported to undergo nucleation and form fibrous projections that result in cell-death. In living system (microorganisms and higher organisms alike), similar functional amyloid proteins are known to be produced with similar nucleation processes. A major amyloid involved in Alzheimer’s disease (AD) is the misfolding of human a-synuclein (2N0A). In this report the homologous protein of 2N0A was created and studied for interaction with functional amyloid, TasA from Bacillus subtilis (5OF1) using the Z-dock server, and analyzed the interacting aminoacids. This report will help in understanding the self-folding and nucleation process of the functional amyloids in bacteria and further correlate their interaction with human pathological amyloids.

Keywords: Functional amyloids, homology modelling, docking, interaction, Alzheimer’s disease (AD)