ArticleBiomolecules2019
Unraveling Binding Mechanism of Alzheimer's Drug Rivastigmine Tartrate with Human Transferrin: Molecular Docking and Multi-Spectroscopic Approach towards Neurodegenerative Diseases.
Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 67 citations in OpenAlex.
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- Exploring the binding of cinchonine with human transferrin: combined experimental and computational approaches.Scientific reports · 2025Article
- Computational drug repurposing reveals Alectinib as a potential lead targeting Cathepsin S for therapeutic developments against cancer and chronic pain.Frontiers in bioinformatics · 2025Article
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- Alzheimer's Disease-Biochemical and Psychological Background for Diagnosis and Treatment.International journal of molecular sciences · 2023Review
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- Binding Studies of Caffeic and p-Coumaric Acid with α-Amylase: Multispectroscopic and Computational Approaches Deciphering the Effect on Advanced Glycation End Products (AGEs).Molecules (Basel, Switzerland) · 2022Article
- Unraveling the Binding Mechanism of Alzheimer's Drugs with Irisin: Spectroscopic, Calorimetric, and Computational Approaches.International journal of molecular sciences · 2022Article
- Antidiabetic Drugs in the Treatment of Alzheimer's Disease.International journal of molecular sciences · 2022Review
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Studying drug-protein interactions has gained significant attention lately, and this is because the majority of drugs interact with proteins, thereby altering their structure and, moreover, their functionality. Rivastigmine tartrate (RT) is a drug that is in use for mild to moderate Alzheimer therapy. This study was targeted to characterize the interaction between human transferrin (hTf) and RT by employing spectroscopy, isothermal titration calorimetry (ITC), and molecular docking studies. Experimental results of fluorescence quenching of hTf induced by RT implied the formation of a static complex between hTf and RT. Further elucidation of the observed fluorescence data retorting Stern-Volmer and modified Stern-Volmer resulted in binding constants for hTf-RT complex of the order 10
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Registered trials
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