Computational analysis of structural features in tetrameric amyloid β1-42 peptides containing <scp>D-</scp> Asp1, 7, and 23 residues
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.
Authors
- Akifumi Oda (ORCID: https://orcid.org/0000-0001-6487-7977)
- Tomoki Nakayoshi (ORCID: https://orcid.org/0000-0002-2905-3611)
- Koichi Kato (ORCID: https://orcid.org/0000-0001-6984-2343)
- Ayato Mizuno
- Kenju Inaoka
- Ayumi Shingaki
Institutions
- Shonan University of Medical Sciences (JP)
- Protein Research Foundation (JP)
- Nagoya University (JP)
- Meijo University (JP)
- The University of Osaka (JP)
Publication Details
- Journal
- Chemistry Letters
- Published
- 2026-02-01
- DOI
- https://doi.org/10.1093/chemle/upag015
- Primary Topic
- Alzheimer's disease research and treatments
- Type
- article
- Field-Weighted Citation Impact
- 0.00