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- W4313410370 abstract "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." @default.
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- W4313410370 date "2023-01-01" @default.
- W4313410370 modified "2023-10-02" @default.
- W4313410370 title "A biophysical approach of cytarabine anticancer drug insights into human serum albumin and checkpoint kinase 1" @default.
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- W4313410370 doi "https://doi.org/10.1016/j.rechem.2022.100755" @default.
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