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<p>The interaction between drugs and biological receptors, such as proteins and DNA, is crucial for understanding their biological activities. Human serum albumin (HSA) is a widely used protein for studying molecular interactions. Riluzole (RLZ), a benzothiazole-containing drug, treats amyotrophic lateral sclerosis and motor neuron diseases, and has neuroprotective effects. This study investigates the interaction between RLZ and HSA, examining the effects on biomolecular structure. Using UV–visible and fluorescence spectroscopy, we determined the equilibrium binding constant (K<sub>b</sub>), number of binding sites (n), quenching constant (K<sub>SV</sub>) and bimolecular quenching constant (Kq). The results show that the binding and quenching constants are in the order of 10<sup>4</sup> and 10<sup>3</sup>&#xa0;M<sup>−1</sup>, respectively. Displacement studies with site-specific markers (warfarin, ANS, and ibuprofen) revealed the binding of RLZ in subdomain IIIA of HSA. Circular dichroism (CD) experiments showed no binding-induced structural changes in HSA, while induced CD of RLZ further supports the binding. Molecular docking simulations supported the experimental findings, showing the binding location of RLZ in subdomain IIIA of HSA. Thus, the study revealed the binding of RLZ with HSA with no effect of RLZ on the secondary structure of the protein. This study may provide an insight to understand better on the molecular interactions of RLZ related structures with HSA, and further may help in potential drug development.</p>

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Interaction between Riluzole and Human Serum Albumin: A Biophysical Study

  • 期刊论文

  • 发表日期：

    2025年9月17日

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  • Ragaiahgari Srinivas Reddy,
  • Bijaya Ketan Sahoo,
  • Anna Tanuja Safala Bodapati,
  • Shravya Rao Madku,
  • Kandikonda Lavanya

摘要

The interaction between drugs and biological receptors, such as proteins and DNA, is crucial for understanding their biological activities. Human serum albumin (HSA) is a widely used protein for studying molecular interactions. Riluzole (RLZ), a benzothiazole-containing drug, treats amyotrophic lateral sclerosis and motor neuron diseases, and has neuroprotective effects. This study investigates the interaction between RLZ and HSA, examining the effects on biomolecular structure. Using UV–visible and fluorescence spectroscopy, we determined the equilibrium binding constant (Kb), number of binding sites (n), quenching constant (KSV) and bimolecular quenching constant (Kq). The results show that the binding and quenching constants are in the order of 104 and 103 M−1, respectively. Displacement studies with site-specific markers (warfarin, ANS, and ibuprofen) revealed the binding of RLZ in subdomain IIIA of HSA. Circular dichroism (CD) experiments showed no binding-induced structural changes in HSA, while induced CD of RLZ further supports the binding. Molecular docking simulations supported the experimental findings, showing the binding location of RLZ in subdomain IIIA of HSA. Thus, the study revealed the binding of RLZ with HSA with no effect of RLZ on the secondary structure of the protein. This study may provide an insight to understand better on the molecular interactions of RLZ related structures with HSA, and further may help in potential drug development.