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Date Published: 14/03/2023
Online Published: 14/03/2023
Abstract Views: 114
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DOI: https://doi.org/10.52714/dthu.12.2.2023.1031
Issue
Vol. 12 No. 2 (2023): Natural Sciences Issue (Vietnamese)
Section
Natural Sciences Issue (Vietnamese)
How to Cite
Huynh, T. N. T., Nguyen, Q. T., & Bui, V. T. (2023). Studying the interaction of CID 16040294 compound with beta amyloid by docking method. Dong Thap University Journal of Science, 12(2), 44-49. https://doi.org/10.52714/dthu.12.2.2023.1031

Studying the interaction of CID 16040294 compound with beta amyloid by docking method

Thi Ngoc Thanh Huynh1, Quoc Thai Nguyen2, , Van Thang Bui3
1 IT and Lab Center, Dong Thap University, Vietnam
2 Department of Natural Sciences Teacher Education, Dong Thap University, Vietnam
3 Academic Aff airs Offi ce, Dong Thap University, Vietnam

Main Article Content

Abstract

The amyloid hypothesis admits that the Alzheimer’s disease etiology is associated with selfassembly of amyloid beta (Aβ) peptides inside the brain. The Aβ peptides are produced by proteolytic cleavage of the amyloid precursor protein (APP) by β-secretase and γ-secretase. Among these, Aβ42 is more toxic than Aβ40 and is the cause of neuronal cell death. Using docking simulation, the interaction of CID 16040294 (GVD) with Aβ42 fibrils was investigated. The results show that CID 16040294 (GVD) strongly interacts with Aβ42 fibrils, interacts best with the 2MXU fibril structure, and the non-binding interaction plays a more important role than Hydrogen bonding in the steady state of the receptor-ligand conformation. From these results, we propose that GVD compound is a potential compound to treat Alzheimer’s disease.

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Creative Commons License

This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.

Keywords

Amyloid beta, Alzheimer's disease, docking method, binding free energy

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