Molecular-dynamics simulations for amyloid beta 1-42 monomer with D-aspartic acid residues using continuous solvent.
Molecular-dynamics simulations of amyloid-beta(1-42) peptides including D-aspartic acid residues were performed, and their three-dimensional structures were compared. The simulations were performed in an aqueous environment using a continuous solvent model. In the structures obtained from simulations, the occurrence ratio of beta-extended structures for the peptide that included D-Asp23 was larger than that for the wild-type peptide. These beta-extended structures appeared in the C-terminal region of the peptide, and the alpha-helix structures of the region were lost. On the other hand, for the peptide that included the stereo-inverted form of Asp1 as well as D-Asp23, the occurrence ratio of beta-extended structures in the C-terminal region was lower than that of the peptide including only D-Asp23.
Oda
Akifumi
A
Faculty of Pharmaceutical Sciences, Tohoku Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai, Miyagi 981-8558, Japan. oda@tohoku-pharm.ac.jp
Kobayashi
Kana
K
Takahashi
Ohgi
O
D016229:Amyloid beta-Peptides / Q000737:chemistry*; D026603:D-Aspartic Acid / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012997:Solvents / Q000737:chemistry*; D013237:Stereoisomerism
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; D012997:Solvents; C075222:amyloid beta-protein (1-42); D026603:D-Aspartic Acid