4.2 Article

Fabrication of Reduced Graphene Oxide-Ag Nanocomposites and Analysis on the Interaction with BSA

期刊

JOURNAL OF NANOMATERIALS
卷 2019, 期 -, 页码 -

出版社

HINDAWI LTD
DOI: 10.1155/2019/2707909

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资金

  1. National Natural Science Foundation of China [81502255, 21603084]
  2. Natural Science Foundation of Shandong Province [ZR2017BB015, ZR2016BP10, ZR2018PB011]
  3. Medicine and Health Project of Shandong Province [2016WS0164]
  4. Higher Education Research Project of Shandong Province [J17KB065]
  5. School Support Foundation of Jining Medical University [JY2017KJ042]
  6. NSFC cultivation project of Jining Medical University [JYP20418KJ03, JYP20418KJ17]
  7. Staring Foundation of Affiliated Hospital of Jining Medical University [2016-BS-009]
  8. Science and Technology Development Plan Foundation of Jining [2014jnjc09]
  9. School-Level University Student Research Project [JYXS2017KJ007]
  10. National College/School-Level Students Innovation and Entrepreneurship Training Program [cx2018008, 201810443008]

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Graphene is an excellent platform to support and stabilize silver nanoparticles (AgNPs). The reduced graphene oxide-silver nanoparticles (rGO-AgNPs) were synthesized by the chemical reduction method and characterized by using ultraviolet-visible (UV-vis) absorption, transmission electron microscopy (TEM), X-ray diffractometer (XRD), and scanning probe microscopy (SPM). The binding reaction of rGO-AgNPs with bovine serum albumin (BSA) was investigated by using fluorescence spectrometry and SPM. As the concentration of AgNPs increased, the fluorescence spectrum was quenched, and the quenching process of rGO-AgNPs and BSA was static quenching. Thermodynamic parameters of the absorption process were evaluated at different temperatures, and the negative values of Gibbs free energy (Delta G) showed that this process was spontaneous. The main type of interaction was hydrophobic interaction according to the values of changes in standard enthalpy (Delta H) and entropy (Delta S). In addition, the morphology changes of proteins interacting with nanomaterials were detected by SPM.

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