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<p>Timolol maleate (TM), a beta-blocker drug, is used in treating conditions related to arterial hypertension. Exploring the possible interaction between TM and plasma proteins is crucial for enhancing the drug potency. This interaction study is done to examine the impact of TM on the comportment of bovine plasma Fibrinogen (FB) by utilizing spectroscopic and computational techniques such as fluorescence spectroscopy, circular dichroism (CD), and molecular docking. Employing fluorescence spectroscopy at temperatures 290&#xa0;K, 298&#xa0;K, and 308&#xa0;K disclosed that TM used hydrophobic interactions to quench the intrinsic fluorescence of FB and show a hypochromic shift. The values of the binding and quenching rate constant specify the strong interaction between the TM and FB. The thermodynamic parameters such as ΔH and ΔG unveil the existence of hydrophobic forces. The CD demonstrates the influence of TM on the secondary structure of FB. Molecular docking revealed the theoretical evaluation of FB and TM binding. The investigation provides insightful information on stability, pharmacokinetics and bioavailability of TM, which is crucial for maximizing its therapeutic value.</p>

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Insights into the interaction of Fibrinogen with Timolol Maleate and elucidation of binding sites via. spectroscopic and molecular docking study

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年8月27日

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  • Neha Govind Rao,
  • Anu Radha Pathania,
  • Harman Deep Kour,
  • Suhas Ballal,
  • Abhayveer Singh,
  • Abhijit Bhowmik,
  • Balewgize Amare Zeru

摘要

Timolol maleate (TM), a beta-blocker drug, is used in treating conditions related to arterial hypertension. Exploring the possible interaction between TM and plasma proteins is crucial for enhancing the drug potency. This interaction study is done to examine the impact of TM on the comportment of bovine plasma Fibrinogen (FB) by utilizing spectroscopic and computational techniques such as fluorescence spectroscopy, circular dichroism (CD), and molecular docking. Employing fluorescence spectroscopy at temperatures 290 K, 298 K, and 308 K disclosed that TM used hydrophobic interactions to quench the intrinsic fluorescence of FB and show a hypochromic shift. The values of the binding and quenching rate constant specify the strong interaction between the TM and FB. The thermodynamic parameters such as ΔH and ΔG unveil the existence of hydrophobic forces. The CD demonstrates the influence of TM on the secondary structure of FB. Molecular docking revealed the theoretical evaluation of FB and TM binding. The investigation provides insightful information on stability, pharmacokinetics and bioavailability of TM, which is crucial for maximizing its therapeutic value.