ArticleScientific reports2021
Interaction study of monoisoamyl dimercaptosuccinic acid with bovine serum albumin using biophysical and molecular docking approaches.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 28 citations in OpenAlex.
- Pyridoxal-Based Selective Chemo Sensor for Colorimetric and Fluorescent Detection of Copper Ions and Imaging in Live Cells.Journal of fluorescence · 2026Article
- HAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- A Glucose-Responsive CeO₂@GOx Nanozyme Embedded in Chitosan/PVA Hydrogel for Accelerated Diabetic Wound Healing: from Molecular Simulations toNanotheranostics · 2026Article
- Insights into the Binding of Metadoxine with Bovine Serum Albumin: A Multi-Spectroscopic Investigation Combined with Molecular Docking.Current protein & peptide science · 2025Article
- Article
- Heme Protein Binding of Sulfonamide Compounds: A Correlation Study by Spectroscopic, Calorimetric, and Computational Methods.ACS omega · 2022Article
- Interaction Study between ESIPT Fluorescent Lipophile-Based Benzazoles and BSA.Molecules (Basel, Switzerland) · 2021Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Monoisoamyl 2,3-dimercaptosuccinic acid (MiADMSA), a lipophilic chelator has been evaluated for its potential use as an antidote in arsenic poisoning. The pharmacokinetics and pharmacodynamics properties of a drug could be understood via study its mechanism of interaction with bovine serum albumin protein (BSA). Therefore, the interaction between MiADMSA with BSA was investigated using various spectroscopic techniques and computational methods. Linear quenching of BSA intrinsic fluorescence intensity with the increasing concentration of MiADMSA was observed in the fluorescence study. Furthermore, synchronous results revealed that MiADMSA slightly changed the conformation of BSA. The binding constant value of the BSA-MiADMSA complex was found 1.60 × 10
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