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Open Access
Original Research
Search for potential Alzheimer disease Therapeutics: Identification of inhibitors of amyloid oligomerization with high affinity for the Zinc binding site
Elizaveta Lugovskaya; Giulia Codagnone; Ivan Sanavia; Silvia Rey; Vanessa Terranova; Marcello Miceli; Marco A. Deriu and Jack Adam Tuszynski
Author Affiliations
Elizaveta Lugovskaya: Department of Mechanical and Aerospace Engineering, Politecnico di Torino, Corso Duca degli Abruzzi 24, IT-10128 Torino, Italy.
Giulia Codagnone: Department of Mechanical and Aerospace Engineering, Politecnico di Torino, Corso Duca degli Abruzzi 24, IT-10128 Torino, Italy.
Ivan Sanavia: Department of Mechanical and Aerospace Engineering, Politecnico di Torino, Corso Duca degli Abruzzi 24, IT-10128 Torino, Italy.
Silvia Rey Vanessa Terranova: Department of Mechanical and Aerospace Engineering, Politecnico di Torino, Corso Duca degli Abruzzi 24, IT-10128 Torino, Italy.
Marcello Miceli: Department of Mechanical and Aerospace Engineering, Politecnico di Torino, Corso Duca degli Abruzzi 24, IT-10128 Torino, Italy.
Marco A. Deriu: Department of Mechanical and Aerospace Engineering, Politecnico di Torino, Corso Duca degli Abruzzi 24, IT-10128 Torino, Italy.
Jack Adam Tuszynski:
Department of Mechanical and Aerospace Engineering, Politecnico di Torino, Corso Duca degli Abruzzi 24, IT-10128 Torino, Italy.
Department of Data Science and Engineering, The Silesian University of Technology, Gliwice, Poland .
Department of Physics, University of Alberta, Edmonton, AB T6G 2R3, Canada.
Abstract
The progression of Aβ peptide aggregation in the brain has been suggested to play an important role in the pathogenesis and development of Alzheimer’s disease. The present study is intended to provide insight into the interactions between the zinc binding site of beta-amyloids and the zinc ion itself. It has been amply demonstrated that the absence of zinc bonded to the beta-amyloid may slow down the progression of the Alzheimer disease, so the goal is to provide an analysis of available drugs that can be repurposed, while waiting for the development of novel therapeutics. To this end, we address the issues of how and with what strength the existing compounds bind with beta-amyloid, potentially replacing or blocking zinc and preventing it from attaching to the amyloid itself. The analysis was performed using MOE software which, starting from a filtered database, made it possible to identify the drugs that were most likely to bind to the zinc binding site on beta-amyloid.
Keywords
Amyloid Beta; Zinc Binding Site; Lipinski Rule of Five; Molecular Docking.
How to cite this article
Elizaveta Lugovskaya, Giulia Codagnone, Ivan Sanavia, Silvia Rey, Vanessa Terranova, Marcello Miceli, Marco A. Deriu and Jack Adam Tuszynski (2024). Search for potential Alzheimer Disease therapeutics: Identification of inhibitors of amyloid oligomerization with high affinity for the Zinc binding site. Journal of Multiscale Neuroscience 3(3), 186-199.
Conflict of Interest
The authors declare no conflict of interest.
Copyright
© 2024 The Author(s). Published by Neural Press. This is an open access article distributed under the terms and conditions of the CC BY 4.0 license.
Disclaimer
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