RESEARCH ARTICLE
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Identification of key stabilizing interactions of amyloid-β oligomers based on fragment molecular orbital calculations on macrocyclic β-hairpin peptides
Rohoullah Firouzi,
Bahare Noohi,
Corresponding Author
Rohoullah Firouzi
Department of Physical Chemistry, Chemistry and Chemical Engineering Research Center of Iran, Tehran, Iran
Correspondence
Rohoullah Firouzi, Department of Physical Chemistry, Chemistry and Chemical Engineering Research Center of Iran, Tehran, Iran.
Email: [email protected]
Search for more papers by this authorBahare Noohi
Department of Physical Chemistry, Chemistry and Chemical Engineering Research Center of Iran, Tehran, Iran
Search for more papers by this authorRohoullah Firouzi,
Bahare Noohi,
Corresponding Author
Rohoullah Firouzi
Department of Physical Chemistry, Chemistry and Chemical Engineering Research Center of Iran, Tehran, Iran
Correspondence
Rohoullah Firouzi, Department of Physical Chemistry, Chemistry and Chemical Engineering Research Center of Iran, Tehran, Iran.
Email: [email protected]
Search for more papers by this authorBahare Noohi
Department of Physical Chemistry, Chemistry and Chemical Engineering Research Center of Iran, Tehran, Iran
Search for more papers by this authorAbstract
Analyzing the electronic states and inter-/intra-molecular interactions of amyloid oligomers expand our understanding of the molecular basis of Alzheimer's disease and other amyloid diseases. In the current study, several high-resolution crystal structures of oligomeric assemblies of Aβ-derived peptides have been studied by the ab initio fragment molecular orbital (FMO) method. The FMO method provides comprehensive details of the molecular interactions between the residues of the amyloid oligomers at the quantum mechanical level. Based on the calculations, two sequential aromatic residues (F19 and F20) and negatively charged E22 on the central region of Aβ have been identified as key residues in oligomer stabilization and potential interesting pharmacophores for preventing oligomer formation.
CONFLICT OF INTEREST
The authors declare no conflict of interest.
Open Research
DATA AVAILABILITY STATEMENT
The data that supports the findings of this study are openly available in the supplementary material of this article.
Supporting Information
| Filename | Description |
|---|---|
| prot26212-sup-0001-supinfo.docxWord 2007 document , 5 MB | APPENDIX S1: Supporting information |
Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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