Version 1
: Received: 14 December 2023 / Approved: 15 December 2023 / Online: 15 December 2023 (14:59:46 CET)
How to cite:
FERRARI, I.V. Exploring the Therapeutic Potential of Hypericin: Molecular Docking with ABAD and BACE1 targets in Alzheimer's Disease Pathogenesis. Preprints2023, 2023121188. https://doi.org/10.20944/preprints202312.1188.v1
FERRARI, I.V. Exploring the Therapeutic Potential of Hypericin: Molecular Docking with ABAD and BACE1 targets in Alzheimer's Disease Pathogenesis. Preprints 2023, 2023121188. https://doi.org/10.20944/preprints202312.1188.v1
FERRARI, I.V. Exploring the Therapeutic Potential of Hypericin: Molecular Docking with ABAD and BACE1 targets in Alzheimer's Disease Pathogenesis. Preprints2023, 2023121188. https://doi.org/10.20944/preprints202312.1188.v1
APA Style
FERRARI, I.V. (2023). <strong> </strong> Exploring the Therapeutic Potential of Hypericin: Molecular Docking with ABAD and BACE1 targets in Alzheimer's Disease Pathogenesis. Preprints. https://doi.org/10.20944/preprints202312.1188.v1
Chicago/Turabian Style
FERRARI, I.V. 2023 "<strong> </strong> Exploring the Therapeutic Potential of Hypericin: Molecular Docking with ABAD and BACE1 targets in Alzheimer's Disease Pathogenesis" Preprints. https://doi.org/10.20944/preprints202312.1188.v1
Abstract
This study employs molecular docking experiments to investigate the binding interactions of Hypericin with key proteins implicated in Alzheimer's disease (AD). Hypericin demonstrated a significant binding energy of -10.1 kcal/mol with ABAD (3-hydroxyacyl-CoA dehydrogenase type II). The analysis revealed multiple binding interactions, including hydrogen bonds with arginine 6, serine 7, and glutamic acid 140, as well as hydrophobic bonds involving leucine 11, aspartic acid 142, and aspartic acid 86. These findings illuminate the intricate molecular interactions between Hypericin and ABAD, suggesting its potential as a lead compound for further therapeutic development in the context of Alzheimer's disease. Additionally, a parallel docking investigation was conducted for Beta-secretase 1 (BACE1), a protein pivotal in the generation of beta-amyloid peptides—a hallmark of Alzheimer's disease. Inhibiting BACE1 activity is considered a promising therapeutic strategy for AD. Computational analyses suggest that Hypericin may serve as a potential inhibitor of BACE1. Molecular Docking results reveal a robust binding affinity between Hypericin and BACE1, supported by a significant binding energy score of -10.3 kcal/mol. Notably, both ABAD and BACE1 exhibit high binding affinity with Hypericin. This theoretical exploration provides an initial understanding of the intricate molecular pathways involved in Alzheimer's disease and proposes Hypericin as a potential therapeutic compound for mitigating its progression.
Keywords
Alzheimer's disease; Molecular Docking; Hypericin; BACE1; ABAD (3-hydroxyacyl-CoA dehydrogenase type II
Subject
Medicine and Pharmacology, Neuroscience and Neurology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
