Conformational particularities of beta-amyloid peptide 25-35
- Autores: Agaeva G.1, Najafova G.2
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Afiliações:
- Baku State University
- French-Azerbaijani University
- Edição: Volume 68, Nº 5 (2023)
- Páginas: 871-877
- Seção: Articles
- URL: https://journals.rcsi.science/0006-3029/article/view/233449
- DOI: https://doi.org/10.31857/S0006302923050058
- EDN: https://elibrary.ru/PGRHNS
- ID: 233449
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Resumo
In Alzheimer's disease, beta-amyloid peptide (Ав) plays an important role in the mechanism of neurodegeneration. A small fragment of Лв(25-35) (with the sequence GSNKGAIIGLLM) is regarded to be the functional domain of Лв, responsible for its neurotoxic properties and represents the biological active region of Лв. Conformational analysis of each C-terminal segment of the peptide by the method of molecular mechanics revealed a limited number of most probable conformations and quite clearly helped to clarify what forces stabilize the structures. The obtained results showed that Лв(25-35) energetically has a propensity for adopting alpha-helix conformation of the C-terminal octapeptide segment. A molecular dynamics method was used to build a model of intramolecular mobility in the Лв(25-35) molecule. It was demonstrated that in low-energy conformations, Лв(25-35), the orientation of flexible structures of the N-terminal region with respect to the structures of the C-terminal region is different.
Sobre autores
G. Agaeva
Baku State University
Email: gulshen@mail.ru
Baku, Azerbaijan
G. Najafova
French-Azerbaijani UniversityBaku, Azerbaijan
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