Biophysical Chemistry Laboratory, Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.
Centre for Nano and Material Sciences, Jain University, Jain Global Campus, Bengaluru, India.
J Mol Recognit. 2020 Aug;33(8):e2841. doi: 10.1002/jmr.2841. Epub 2020 Mar 9.
To get an idea about the pharmacokinetics and pharmacodynamics, it is important to study the drug-protein interaction. Therefore, herein, we studied the interaction of diclofenac sodium (DIC) with human hemoglobin. The binding study of nonsteroidal antiinflammatory drug, DIC with human hemoglobin (HHB) was done by utilizing fluorescence, UV-visible, time-resolved fluorescence and far-UV circular dichroism spectroscopy (CD). Various thermodynamic parameters such as enthalpy change (ΔH), entropy change (ΔS), and Gibbs free energy change (ΔG) were also calculated. CD results showed that DIC induces secondary structure change in HHB. Fluorescence resonance energy transfer was also performed. Additionally, it was also observed that DIC inhibits the esterase-like enzymatic activity of HHB via competitive inhibition.
为了了解药物的药代动力学和药效动力学，研究药物-蛋白相互作用很重要。因此，在本文中，我们研究了二氯芬酸钠（DIC）与人血红蛋白的相互作用。通过荧光、紫外可见、时间分辨荧光和远紫外圆二色性光谱（CD）研究了非甾体抗炎药 DIC 与人血红蛋白（HHB）的结合。还计算了各种热力学参数，如焓变（ΔH）、熵变（ΔS）和吉布斯自由能变（ΔG）。CD 结果表明，DIC 诱导 HHB 的二级结构发生变化。还进行了荧光共振能量转移。此外，还观察到 DIC 通过竞争性抑制抑制 HHB 的酯酶样酶活性。
