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Yue, Y., Chen, X., Qin, J. and Yao, X. (2009) Spectroscopic Investigation on the Binding of Antineoplastic Drug Oxaliplatin to Human Serum Albumin and Molecular Modeling. Colloids and Surfaces B: Biointerfaces, 69, 51-57.
https://doi.org/10.1016/j.colsurfb.2008.10.016

has been cited by the following article:

• TITLE: Fluorescence Spectroscopy and Molecular Docking Approach to Probe the Interaction between Dehydroeburicoic Acid and Human Serum Albumin

  AUTHORS: Shijie Zheng, Shude Yang, Xianhao Cheng, Tolgor Bau, Yu Li, Rui Zhang, Haiying Bao

  KEYWORDS: Human Serum Albumin, Dehydroeburicoic Acid, Interaction, Fluorescence, Molecular Docking

  JOURNAL NAME: Advances in Microbiology, Vol.9 No.1, January 14, 2019

  ABSTRACT: The interaction between dehydroeburicoic acid (DeEA), a triterpene purified from medicinal fungi and the major transport protein, human serum albumin (HSA), were systematically studied by fluorescence spectroscopy, synchronous fluorescence spectroscopy, three-dimensional fluorescence spectroscopy and molecular docking approach under simulated physiological conditions. The intrinsic fluorescence of HSA was quenched through the combination of static and dynamic quenching mechanism. DeEA cannot be stored and carried by HSA in the body at higher temperature. The hydrogen bonding, hydrophobic force and van der Waals force were major acting forces. The site II was the major binding site. The energy transfer could occur with high probability and the binding distance was 3.29 nm. The binding process slightly changed the conformation and microenvironment of HSA. The DeEA molecule entered the hydrophobic cleft of HSA and formed the hydrogen bonding with Glu-492 and Lys-545.