期刊
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
卷 206, 期 -, 页码 126-134出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2018.07.100
关键词
Niraparib; Human serum albumin; Fluorescence; Molecular docking; Molecular dynamics simulation
类别
资金
- Sichuan Science and Technology Program [2018JY0188]
- Fundamental Research Funds for the Central Universities [2018SCU12043]
- Postdoctoral Foundation of Sichuan University
- Large-scientific Instruments Sharing Platform Ability Construction of Sichuan Province [20161KJTS0037]
- Applied Basic Research Project of Sichuan Province [2018JY0151]
The interactions between 2-{4-[(3S)-piperidin-3-yl] phenyl}-2H-indazole-7-carboxamide (niraparib) and human serum albumin (HSA) were investigated through fluorescence and computational studies. Fluorescence experiments showed that the static quenching mechanism and the binding constant of the HSA-niraparib system at a single binding site was approximately 4 x 10(4) Lmol(-1). Thermodynamic constants indicated that the binding of niraparib to HSA was mainly driven by electrostatic interactions. Competition experiments and molecular docking simulations revealed that niraparib bound to site III of HSA. Synchronous fluorescence and Fourier transform infrared spectroscopy (FT-IR) results suggested that interactions between niraparib and HSA could affect the conformation and microenvironment of HSA. Circular dichroism (CD) measurements revealed that the alpha-helix contents of HSA negligibly increased after binding with niraparib. Molecular dynamics simulations demonstrated the stability of the binary HSA-niraparib system and confirmed that electrostatic forces accounted for the dominant contribution to system energy between HSA and niraparib. (C) 2018 Elsevier B.V. All rights reserved.
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