دورية أكاديمية
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An exploration of binding of Hesperidin, Rutin, and Thymoquinone to acetylcholinesterase enzyme using multi-level computational approaches.

التفاصيل البيبلوغرافية
العنوان: An exploration of binding of Hesperidin, Rutin, and Thymoquinone to acetylcholinesterase enzyme using multi-level computational approaches.
المؤلفون: Mir SA; School of Life Sciences, Sambalpur University, Jyoti Vihar, Odisha, India., Nayak B; School of Life Sciences, Sambalpur University, Jyoti Vihar, Odisha, India., Khan A; Department of Biosciences, Faculty of Science, Integral University, Lucknow, India., Khan MI; Department of Biochemistry, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia.; Centre for Artificial Intelligence in Precision Medicines, King Abdulaziz University, Jeddah, Saudi Arabia., Eldakhakhny BM; Department of Clinical Biochemistry, Faculty of Medicine, King Abdulaziz University, Jeddah, Saudi Arabia., Arif DO; Faculty of Medicine, Ibn Sina National College, Jeddah, Saudi Arabia.
المصدر: Journal of biomolecular structure & dynamics [J Biomol Struct Dyn] 2023 Oct 09, pp. 1-15. Date of Electronic Publication: 2023 Oct 09.
Publication Model: Ahead of Print
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Taylor & Francis Country of Publication: England NLM ID: 8404176 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1538-0254 (Electronic) Linking ISSN: 07391102 NLM ISO Abbreviation: J Biomol Struct Dyn Subsets: MEDLINE
أسماء مطبوعة: Publication: June 2012- : Oxon, UK : Taylor & Francis
Original Publication: Guilderland, NY : Adenine Press, [c1983-
مستخلص: Alzheimer's disease, an intricate neurological disorder, is impacting an ever-increasing number of individuals globally, particularly among the aging population. For several decades phytochemicals were used as Ayurveda to treat both communicable and non-communicable diseases. Acetylcholinesterase (AChE) is a widely chosen therapeutic target for the development of early prevention and effective management of neurodegenerative diseases. The primary objective of the present study was to investigate the binding potential between Rutin Thymoquinone, Hesperidin and the FDA-approved drug Donepezil with AChE. Additionally, a comparative analysis was conducted. These phytochemicals were docked with the binding site of the AChE experimental complex. The molecular dockings demonstrated that the Hesperidinh showed a better binding affinity of -22.0631 kcal/mol. The ADME/T investigations revealed that the selected phytochemicals are non-toxic and drug-like candidates. Molecular dynamics simulations were implemented to determine the conformational changes of Rutin, hesperidin, Thymoquinone, and Donepezil complexed with AChE. Hesperidin and Donepezil were more stable than Rutin, Thymoquinone complexed with AChE. Next, essential dynamics and defining the secondary structure of protein were to determine the conformational changes in AChE complexed with selected phytochemicals during simulations. Overall, the MD Simulations demonstrated that all complexes in this study achieved stability until 100 ns of the simulation period was performed thrice. The structural analysis of AChE was done using multiple search engines to explore the molecular functions, biological processes, and pathways in which AChE proteins are involved and to identify potential drug targets for various diseases. This present study concludes that Hesperidin was found to be a more potent AChE inhibitors than Rutin, and further experiments are required to determine the effectivity of Hesperidin against neurodegenerative diseases.Communicated by Ramaswamy H. Sarma.
فهرسة مساهمة: Keywords: AChE; ADME/T; Phytochemicals; molecular dockings: MD simulations
تواريخ الأحداث: Date Created: 20231009 Latest Revision: 20231009
رمز التحديث: 20240628
DOI: 10.1080/07391102.2023.2265492
PMID: 37811769
قاعدة البيانات: MEDLINE
الوصف
تدمد:1538-0254
DOI:10.1080/07391102.2023.2265492