Simulation of the Lipophilic and Antigenic Cores of the Aβ(1–42) Peptide of Alzheimer's Disease

Abstract

The monomeric Aβ(1–42) peptide of Alzheimer's disease was studied. The peptide is an intrinsically soluble peptide; the N-terminal amino acids are more hydrophilic than the amino acids at the C-terminus. A first hydrophobic core was found at the middle area of the residues (GlN15 to Phe19), a second core at the end (Lys28 to Ala41). There is an antigenic potential at the begin of the sequences and the middle region of the Aβ(1–42) peptide. It is suggested that the middle area has an “amyloidogenic potential” by forming noncovalent interactions between paired, antiparallel β-sheet conformations. A perspective in drug research is to develop compounds that inhibit the associations between monomeric β-strains.