人血清白蛋白
圆二色性
氢键
猝灭(荧光)
分子动力学
病毒学
对接(动物)
疏水效应
范德瓦尔斯力
乙型肝炎病毒
蛋白质二级结构
结晶学
化学
生物物理学
荧光
病毒
生物
生物化学
分子
计算化学
有机化学
医学
物理
量子力学
护理部
作者
Mujaheed Abubakar,Saharuddin B. Mohamad,Adyani Azizah Abd Halim,Saad Tayyab
标识
DOI:10.1080/07391102.2024.2311331
摘要
Molecular docking, molecular dynamics (MD) simulation, atomic force microscopy (AFM) and multi-spectroscopic techniques were selected to unveil the molecular association between the hepatitis B virus (HBV) inhibitor, entecavir (ETR), and the major blood plasma transporter, human serum albumin (HSA). The entire docking and simulation analyses recognized ETR binding to subdomain IIA (Site I) of HSA through hydrogen bonds, hydrophobic and van der Waals forces while maintaining the complex's stability throughout the 100 ns. A gradual lessening in the Stern-Volmer quenching constant (Ksv) with rising temperatures registered ETR-induced quenching of HBV fluorescence as static quenching, thus advising complexation between ETR and HSA. The further advocation of this conclusion was seen from a larger value of the biomolecular quenching rate constant ((kq) > 1010 M−1s−1), changes in the spectra (UV-Vis absorption) of HSA following ETR inclusion and ETR-induced swelling of HSA in the AFM results. The ETR appeared to bind to HSA with moderate affinity (Ka=1.87−1.19×104 M−1) at 290, 300 and 310 K. Significant alterations in the protein's secondary and tertiary structures, including changes in the protein's Tyr/Trp microenvironment, were also detected by circular dichroism and three-dimensional fluorescence spectra when the protein was bound to ETR. The findings of the drug displacement study backed the docking results of Site I as ETR's preferred binding site in HSA.
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