IN SILICO ANALYSIS AND DOCKING STUDY OF THE ACTIVE PHYTO COMPOUNDS OF BACOPA MONNIERI AGAINST ALZHEIMER DISEASE

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Year : 2024 | Volume :13 | Issue : 02 | Page : –
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Anushka Sahu,

  1. Student, School of biotechnology, Devi Ahilya Vishwavidyalaya, University in indore, Madhya Pradesh, India

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Objective: Alzheimer is a neurodegenerative disease and is the cause of 60–70% of cases of dementia. It infected a million people worldwide. An effort was undertaken to explore the potential of natural compounds found in Bacopa monnieri, a plant renowned for its extensive medicinal properties in Indian Ayurveda, to combat the disease. This was achieved through molecular docking studies, evaluation of drug-likeness, and comprehensive ADME (absorption, distribution, metabolism, and excretion) analysis, along with toxicity predictions. Methods: The primary β-secretase protein was obtained from the PDB database. Ligands with weak binding affinity and molecules that could interfere with the docking process were excluded. Docking was then performed using the PyRx tool. The pharmacokinetic properties, including absorption, distribution, metabolism, and excretion (ADME), as well as the drug-likeness of the compounds, were assessed utilizing the Swiss-ADME and ChemAGG platforms. Results: Ramachandran plot analysis illustrates the statistical distribution of the backbone dihedral angles ϕ (phi) and ψ (psi), providing insights into the conformational preferences of the protein structure. Molecular docking studies identified that only one compound from Bacopa monnieri exhibits significant binding affinity, potentially inhibiting the β-secretase enzyme by preventing plaque formation. The ADMET analysis, along with drug-likeness and toxicity predictions, confirmed that ascorbic acid is both safe and possesses favorable drug-like characteristics. Conclusion: This study indicates that ascorbic acid demonstrates a specific binding affinity, with the potential to inhibit the β-secretase enzyme. This suggests its potential role in therapeutic strategies for managing Alzheimer’s disease

Keywords: Alzheimer disease (AD), β-secretase (BACE), Baccopa monnieri (BM), Docking, 4ACU, amyloid

[This article belongs to Research & Reviews : Journal of Computational Biology (rrjocb)]

How to cite this article:
Anushka Sahu. IN SILICO ANALYSIS AND DOCKING STUDY OF THE ACTIVE PHYTO COMPOUNDS OF BACOPA MONNIERI AGAINST ALZHEIMER DISEASE. Research & Reviews : Journal of Computational Biology. 2024; 13(02):-.
How to cite this URL:
Anushka Sahu. IN SILICO ANALYSIS AND DOCKING STUDY OF THE ACTIVE PHYTO COMPOUNDS OF BACOPA MONNIERI AGAINST ALZHEIMER DISEASE. Research & Reviews : Journal of Computational Biology. 2024; 13(02):-. Available from: https://journals.stmjournals.com/rrjocb/article=2024/view=0

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References
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  1. Kaynara Trevisan and R. C. Pereira, “Theories of Aging and the Prevalence of Alzheimer’s Disease,” BioMed Research International , vol. 2019, p. 9, 2019.
  2. M. Zvěřová, “Clinical aspects of Alzheimer’s disease,” Science Direct, pp. 3-6, October 2019.
  3. 1. R. K. R. a. M. A. S. Rudy J. Castellani, “Alzheimer Disease,” Dis Mon, p. 56, 2010.
  4.  “Alzheimer’s Disease: Facts & Figures,” BrightFocus Foundation, 5 october 2022. [Online].
  5. Prof Riqiang Yan Prof Robert Vassar, “Targeting the β secretase BACE1 for Alzheimer’s disease therapy,” The Lancet Neurology, vol. 13, no. 3, pp. 319-329, 2014.
  6. S. L. C. a. R. Vassar, “The Alzheimer’s disease β-secretase enzyme, BACE1,” Springer Nature, 2007.
  7. G. Verdile, S. Fuller, C. S. Atwood, S. M. Laws, S. E. Gandy and R. N. Martins, “The role of beta amyloid in Alzheimer’s disease: still a cause of everything or the only one who got caught?,” Pharmacological Research, vol. 50, no. 4, pp. 397-409, 2004.
  8. C. L.-D. U. Z. J. R. P.-P. Steffen Roßner, “Alzheimer’s disease β-secretase BACE1 is not a neuron-specific enzyme,” journal of neurochemistry, vol. 92, no. 2 , pp. 226-334, 2004.
  9. K. A, “The beta-amyloid cascade hypothesis: a sequence of events leading to neurodegeneration in Alzheimer’s disease,” Neurologia i Neurochirurgia Polska, pp. 405-411, 2004.
  10. D. M. Walsh and D. B. Teplow, “Chapter 4 – Alzheimer’s Disease and the Amyloid β-Protein,” in Progress in Molecular Biology and Translational Science,, 2012, p. 107.
  11.  M.Sathya, P. Premkumar and C. Karthick, “BACE1 in Alzheimer’s disease,” Clinica Chimica Acta, vol. 414, pp. 171-178, 2012.
  12. E. L.D and S. C, “Disrupting β-Amyloid Aggregation for Alzheimer Disease Treatment,” Current Topics in Medicinal Chemistry, vol. 7, pp. 115-126, 2007.
  13. J. C. T. D. K. W. S. C. G. E. Cheng-Ying Ho, “Beta-Amyloid, Phospho-Tau and Alpha-Synuclein Deposits Similar to Those in the Brain Are Not Identified in the Eyes of Alzheimer’s and Parkinson’s Disease Patients,” Brain Pathology, vol. 24, no. 1, pp. 25-32, 2013.
  14. N. V, “ORIGIN AND DEVELOPMENT OF AYURVEDA: (A BRIEF HISTORY),” Anc Sci Life, pp. 1-7, 1981.
  15. L.-c. Mishra, B. B. Singh and S. Dagenais, “Ayurveda: A historical perspective and principles of the traditional healthcare system in India,” Alternative Therapies in Health and Medicine;, p. 7, Mar 2001.
  16. L. L. W. Yogini S. Jaiswal, “A glimpse of Ayurveda – The forgotten history and principles of Indian traditional medicine,” Journal of Traditional and Complementary Medicine, vol. 7, no. 1, pp. 50-53, Feb 2016.
  17.  A. A. S. D. B. S. D. I. L. Michelle D. Nemetchek, “The Ayurvedic plant Bacopa monnieri inhibits inflammatory pathways in the brain,” Journal of Ethnopharmacology, vol. 197, pp. 92-100, Feb 2017.
  18. S. C. Tushar Dubey, “Brahmi (Bacopa monnieri): An ayurvedic herb against the Alzheimer’s disease,” Archives of Biochemistry and Biophysics, vol. 676, p. 108153, November 2019.
  19.  A. Russo and F. Borrelli, “Bacopa monniera, a reputed nootropic plant: an overview,” Phytomedicine, vol. 12, no. 4, pp. 305-317, April 2005.
  20. U. A. S. G. D. R. P. R. G. D. D. V. T. A. D. Samarpita Banerjee, “Bacosides from Bacopa monnieri extract: An overview of the effects on neurological disorders,” Phytotherapy Research, vol. 35, no. 10, pp. 5668-5679, July 2021.
  21.  D. B. M. S. B. G. A. P. G. C. M. G. &. J. S. G. Steven Roodenrys Ph.D, “Chronic Effects of Brahmi (Bacopa monnieri) on Human Memory,” Neuropsychopharmacology, pp. 279-281, November 2001.
  22. A. S. N. K. V. T. M. T. Shishir Goswami, “Effect of Bacopa monnieri on Cognitive functions in Alzheimer’s,” International Journal of Collaborative Research on Internal Medicine & Public Health, vol. 3, no. 4, p. 10, April 2011.
  23. K. S. Chaudhari, N. R. Tiwari, R. R. Tiwari and R. S. Sharma, “REVIEW ARTICLES| MAY 12 2017,” Annals of Neurosciences, vol. 27, no. 2, May 2017.
  24. J. W. Z. F. G. G. T. B. H. W. I. S. P. B. H.M. Berman, “The Protein Data Bank,” Nucleic Acids Research, vol. 28, no. 1, pp. 235-242, Jan 2000.
  25.  M. M. W. M. D. S. T. J. M. Laskowski R A, “PROCHECK – a program to check the stereochemical quality of protein structures,” pp. 283-291., 1993.
  26. C. J. C. T. e. a. Kim S, ” PubChem 2023 update,” Nucleic Acids Res, p. 373–380, 2003.
  27. B. M. J. C. M. C. V. T. O’Boyle NM, “Open Babel: An open chemical toolbox,” J Cheminform, pp. 3-33, 2011.
  28.  R. Vassar, “β-Secretase (BACE) as a drug target for alzheimer’s disease,” Science direct, vol. 54, no. 12, pp. 1589-1602, 2002.
  29. T. Wisniewski, G. Ghiso and B. Frangione, “Biology of Aβ Amyloid in Alzheimer’s Disease,” Neurobiology of Disease, vol. 4, no. 5, pp. 313-328, 1997.
Regular Issue Subscription Original Research
Volume 13
Issue 02
Received 09/05/2024
Accepted 08/10/2024
Published 04/11/2024
182

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