Exploring the mechanisms and properties of Auvelity through computational chemistry
Author
Term
4. Term
Education
Publication year
2024
Submitted on
2024-06-02
Pages
47
Abstract
The aim of this thesis was to determine the binding site and mechanism of action of the novel therapeutic drug Auvelity, a mixture of Dextromethorphan and Bupropion, on the N-methyl-D-aspartate receptor. This was achieved by applying computational chemistry methods. The thesis focused on the antagonist Dextromethorphan, and the methods used included molecular docking, molecular dynamics simulations, and molecular mechanics generalized Born surface area calculations. Computational analyses revealed, that Dextromethorphan binds to the amino terminal domain of the receptor with a binding affinity of −10.2kcal/mole. Van der Waal was the primary binding force, alongside electrostatic forces. These findings were compared to that of a well known antagonist, Ketamine, and the results showed similarities in both binding affinity and interaction forces. The simulations further determined, that Ketamine would also bind to the amino terminal domain, which indicated, that both Dextromethorphan and Ketamine would regulate the receptor through allosteric modulation.
Keywords
Auvelity ; DXM ; Ketamin ; MM/GBSA ; MD-simulationer ; Depression
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