Abstract Amyloid β (Aβ) contains three aspartic acid residues, and D-Asp has been detected in Aβ isolated from senile plaques in the brains of patients with Alzheimer's dementia. In this study, we estimated the three-dimensional structure of an artificial Aβ1-42 mutant in which all Asp residues were converted to D-Asp using molecular dynamics simulations. In the results, the influence of stereoinversion at Asp7 and Asp23 on β-sheet formation was stronger than the inhibitory effect of D-Asp1.
Mizuno et al. (Sun,) studied this question.