Abstract

One group of diseases, known as amyloidoses, which includes Alzheimer’s and the transmissible spongiform encephalopathies, involves deposition of aggregated proteins in a variety of tissues. These diseases are particularly intriguing because evidence is accumulating that the formation of the highly organized amyloid aggregates is a generic property of polypeptides, and not simply a feature of the few proteins associated with recognized pathological conditions. Amyloidosis refers to a group of protein folding diseases. Various innocuous and soluble proteins in physiological conditions polymerize to insoluble amyloid fibrils in several serious diseases, including Alzheimer’s disease (AD) and prion diseases. Designed for theab initio quantum mechanical calculations, we used the density functional theory (DFT). In this theoretical study, we used HF and DFT (BLYP, B3LYP) method for calculation energy, chemical shift nucleus magnetic resonance and quantity thermodynamic by DFT-IR and DFT-NMR. The basis set used were STO-3G, 3-21G,6–31G,6–31G* and 6-31G**. The solvation of biomolecules is essential in molecular biology, since diverse processes involve proteins interacting in changing solvent–solute systems. In conclusion, to obtain more information, we calculated thermo chemical parameters to obtain that the dielectric constant of solvents show a significant role in the Aβ1–42.

Key words: Amyloidosis, ab initio quantum mechanical calculations, DFT, dielectric constant.