Molecular‐Dynamics Simulations for Amyloid <i>β</i><sub>1–42</sub> Monomer with <scp>D</scp>‐Aspartic Acid Residues Using Continuous Solvent

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<jats:title>Abstract</jats:title><jats:p>Molecular‐dynamics simulations of amyloid‐<jats:italic>β</jats:italic><jats:sub>1–42</jats:sub> peptides including <jats:sc>D</jats:sc>‐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 <jats:italic>β</jats:italic>‐extended structures for the peptide that included <jats:sc>D</jats:sc>‐Asp23 was larger than that for the wild‐type peptide. These <jats:italic>β</jats:italic>‐extended structures appeared in the C‐terminal region of the peptide, and the <jats:italic>α</jats:italic>‐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 <jats:sc>D</jats:sc>‐Asp23, the occurrence ratio of <jats:italic>β</jats:italic>‐extended structures in the C‐terminal region was lower than that of the peptide including only <jats:sc>D</jats:sc>‐Asp23.</jats:p>

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