Probing the interaction of Rivastigmine Tartrate, an important Alzheimer’s drug, with serum albumin: Attempting treatment of Alzheimer’s disease
Abstract
The present study was aimed at investigating the binding between an important drug of Alzheimer's therapy, Rivastigmine tartrate (RT), with Bovine serum albumin (BSA). BSA is a model protein that is increasingly being used for studies related to drug-protein interaction owing to its structural similarity with human serum albumin (HSA) which is extremely abundant in the circulatory system comprising around 60% of the total plasma protein. Fluorescence spectroscopy implied that complex formation is taking place between BSA and RT; binding constant calculated was of the order of 10 4 M-1 implicative of the strength of this interaction. Fluorescence spectroscopy was carried out at three different temperatures in a bid to find out the operative mode of quenching; static quenching was taking place for RT-BSA interaction with a binding constant of 2.5 × 10 4 M-1 at 298 K. Further, changes in Far UV CD spectra clearly implied that RT induces structural transition in BSA suggestive of RT-BSA complex formation. The negative value of ∆G 0 as obtained from fluorescence spectroscopy and isothermal titration calorimetry (ITC) suggests the reaction to be spontaneous and thermodynamically favorable. Additionally, molecular docking was employed to investigate different forces and critical residues involved in RT-BSA interaction. Furthermore, all-atom molecular dynamics simulation for 50 ns was performed on the BSA-RT complex to investigate its conformational behavior, stability and dynamics.
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Rivastigmine is authorized for use in mild-to-moderate Parkinson's disease dementia and mild-to-moderate AD.
“It is authorized for use in mild-to-moderate Parkinson’s disease dementia and mild-to-moderate AD [116,117,118].”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [118]
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Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease
Thawabteh, A. M., Ghanem, A. W., AbuMadi, S., Thaher, D., Jaghama, W., Karaman, D., & Karaman, R. (2024) · Molecules · doi:10.3390/molecules29215131 · Cited by 56 · see citing works
“It is authorized for use in mild-to-moderate Parkinson’s disease dementia and mild-to-moderate AD [116–118].”
Background
- Authors
- Shamsi, A., Mohammad, T., Anwar, S., Alajmi, M. F., Hussain, A., Hassan, M. I., Ahmad, F., & Islam, A.
- Affiliations
- Jamia Millia Islamia (IN)
- King Saud University (SA)
- Corresponding author
- Islam, Asimul
- ORCID
- Venue
- International Journal of Biological Macromolecules
- Publisher
- Elsevier BV
- Published
- 2020-04
- Volume
- 148
- Pages
- 533-542
- ISSN
- 0141-8130 (ISSN-L)
- OpenAlex
- W2999541087
- Cited by
- 73
- References
- 48
- Citations by year
- 2026: 6 · 2025: 10 · 2024: 6 · 2023: 14 · 2022: 16 · 2021: 12 · 2020: 9
- FWCI
- 4.22
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- International Journal of Biological Macromolecules (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Indian Council of Medical Research (BIC/12(16)/2014, SR/FST/LSI-541/2012)
- Science and Engineering Research Board (2017/000745)
- King Saud University (RSP-2019-122)
- Department of Science and Technology, Ministry of Science and Technology, India
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Health Sciences › Medicine › Pharmacology › Cholinesterase and Neurodegenerative Diseases
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Keywords
- bovine serum albumin, drug-protein binding, Alzheimer's disease, binding constant, static quenching, protein structural transitions, binding thermodynamics, molecular docking, molecular dynamics simulation
- MeSH terms
- Rivastigmine, Algorithms, Alzheimer Disease, Binding Sites, Humans, Hydrogen Bonding, Molecular Conformation, Protein Binding, Serum Albumin, Spectrum Analysis, Structure-Activity Relationship, Thermodynamics, Molecular Dynamics Simulation, Molecular Docking Simulation
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