A biophysical approach of cytarabine anticancer drug insights into human serum albumin and checkpoint kinase 1
A biophysical approach of cytarabine anticancer drug insights into human serum albumin and checkpoint kinase 1
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阿糖胞苷抗癌药物的生物物理方法深入了解人血清白蛋白和检查点激酶 1
DOI：
10.1016/j.rechem.2022.100755
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发表时间：
2023
影响因子：
2.3
通讯作者：
Ganesan Singaravelu
中科院分区：
文献类型：
--
作者：
Rupavarshini Manoharan;Karthikeyan Subramani;Anandh Sundaramoorthy;Ramamoorthi Anitha;Ramakrishnamurthy Suganya;Bharanidharan Ganesan;Aruna Prakasarao;Mangaiyarkarasi Rajendiran;Chinnathambi Shanmugavel;Pandian Ganesh N.;Ganesan Singaravelu
本研究采用生物物理技术研究阿糖胞苷抗癌药物与人血清白蛋白（HSA）和检查点激酶1的结合作用机制。阿糖胞苷-HSA复合物的紫外-可见吸收光谱显示由于阿糖胞苷药物的存在而发生蓝移。荧光光谱结果表明，随着阿糖胞苷在人血清白蛋白中浓度的增加，荧光发生静态猝灭，并计算了不同温度（293 K、298 K、303 K）下的荧光参数、结合常数（K），结果与分子对接结果吻合较好。对HSA和Chk 1蛋白复合物进行了分子对接和分子动力学研究。在继续对接的过程中，我们还在HSA和Chk 1分子的阿糖胞苷药物结合活性位点进行了DFT分析，以了解原子水平上的内部稳定性。
The present studies used biophysical techniques to examine the binding interaction mechanism of cytarabine anticancer drugs with human serum albumin (HSA) and checkpoint kinase 1. The UV–vis absorption spectrum of the cytarabine-HSA complex reveals a blue shift due to the presence of the cytarabine drug. The results of the fluorescence spectroscopy indicate that static quenching happened as the cytarabine drug concentration in HSA was increased and thermodynamical parameters, binding constant (K) were calculated at different temperatures (293 K, 298 K, 303 K) results have good agreement with molecular docking studies. Molecular docking and molecular dynamics studies were carried out for both HSA and Chk1 protein complexes. In continuing with docking, we have also carried out DFT analysis at the cytarabine drug binding active site of HSA and Chk1 molecule to understand the internal stability at the atomic level.