Computational analysis of structural features in tetrameric amyloid β1-42 peptides containing D- Asp1, 7, and 23 residues
Abstract
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.
Fields of Study & Subjects
Alzheimer's disease research and treatments
Protein Structure and Dynamics
Dementia and Cognitive Impairment Research
Publication details
- Journal / source
- Chemistry Letters
- Volume
- 55
- Issue
- 2
- Publication date
- 1 February 2026
- Language
- EN