MOLECULAR DYNAMICS SIMULATION OF CONFORMATIONAL BEHAVIOR OFAMYLOID-β PEPTIDE (25-35)

Abstract

The conformational behavior and flexibility of Amyloid beta-peptide (25-35) have been investigated in a vacuum and in the polar medium using molecular dynamics method. Amyloid peptide (Aβ) is the major component of senile plaques found in the brain of patients of Alzheimer's disease. β-amyloid peptide (25-35) (Aβ25-35) is a biologically active fragment of Aβ. The calculation showed that the spatial structure of this peptide tends to adopt an α-helical conformation from Lys28 to Met35. The conformational behavior of this peptide can be described by a set of similar low-energy conformations having α-helical structure at the C-terminal sequence. The permissible changes of values dihedral angles of Amyloid beta-peptide (25-35) lowest energy conformations and stability of the secondary structure elements have been investigated by molecular dynamics simulation. The comparative study results have shown that the preferred conformations of this molecule are not fully disordered structure in the solvent, but it has a stable helical segment at the C-terminal part of molecules.