4.7 Article

Study on the interaction of graphene oxide silver nanocomposites with bovine serum albumin and the formation of nanoparticle-protein corona

Journal

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 116, Issue -, Pages 492-501

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2018.05.043

Keywords

GO-Ag nanocomposites; Bovine serum albumin; Synchronous fluorescence; Circular dichroism spectra; Three-dimensional fluorescence spectra; Scanning probe microscopy

Funding

  1. National Natural Science Foundation of China [21373106, 81502255]
  2. Natural Science Foundation of Shandong Province [ZR2017BB015, ZR2016BP10, ZR2013HL011]
  3. Medicine and Health Project of Shandong Province [2016WS0164]
  4. Higher Education Research Project of Shandong Province [J17KB065]
  5. Youth Support Foundation of Jining Medical University [JY2017KJ042]
  6. Staring Foundation of Affiliated Hospital of Jining Medical University [2016-BS-009]

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The interaction between graphene oxide-sliver nanocomposites (GO-AgNCPs) and bovine serum albumin (BSA) in aqueous buffer solution was investigated by using several spectroscopic and imaging techniques. The visible absorbance intensity of GO-AgNCPs increased with increasing concentrations of BSA, and a slight redshift of the surface plasmon resonance band (SPR) occurred due to the absorption of BSA on the surface of GO-AgNCPs. Fluorescence data revealed a static quenching process of BSA caused by GO-AgNCPs. Thermodynamic parameters of the absorption process, including adsorption equilibrium constants, changes in Gibbs free energy (Delta G), enthalpy (Delta H) and entropy (Delta S), were evaluated at different temperatures. Negative values of Delta G showed that this process was spontaneous and the BSA-GO-AgNCPs complex might form in aqueous solution. Negative values of Delta H and Delta S suggested that the binding was mainly an enthalpy-driven process, and van der Waals forces and hydrogen bonding were the major force in the formation of the nanoparticle-protein corona. Analysis of synchronous, three dimensional (3D) fluorescence and circular dichroism (CD) spectra demonstrated that the conformation of BSA was slightly altered in the presence of GO-AgNCPs. The protein corona formed on the surface of GO-AgNCPs was directly observed by scanning probe microscopy (SPM). (C) 2018 Elsevier B.V. All rights reserved.

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