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For the g-C3N4/PtNi/GO-0.5 g-C3N4/PtNi/GO-0.5 g-C3N4/PtNi/GO-0.5 of Pt 4f shift about 0.42 eV to high binding energy compared with pure Pt.
The Ag 3d5/2 and 3d3/2 peaks of Ag/rGO nanocomposites 1C appeared at 368 and 374 eV, respectively, which shifted to the lower binding energy compared with the characteristic peaks for silver metal at 368.2 and 374.2 eV.
The peak of O1s from rGO (531.3 eV) shifted to lower binding energy compared with that of GO (531.8 eV), implying that there existed a chemical interaction between rGO and Ag3PO4 QDs by C=O bond.
Furthermore, the binding energies of Ag 3d for Ag-ZnO shift to the lower binding energy compared with bare Ag metal NPs (368.2 and 374.2 eV for Ag 3d5/2 and Ag 3d3/2, respectively) should be caused by the interaction between ZnO NRs and Ag NPs. Figure 5 XPS spectra of samples.
The binding energies of Ag 3d 5/2 and Ag 3d 3/2 for the Ag/ZnO nanocables are 367.7 and 373.7 eV, respectively, which shift remarkably to the lower binding energy compared with the corresponding values of the synthesized pure metallic Ag (the standard binding energies of Ag 3d 5/2 and Ag 3d 3/2 for bulk Ag are about 368.2 and 374.2 eV, respectively).
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Zhang et al. reported that the neutral Ag12V cluster show larger relative binding energies compared with pure icosahedral Ag13 cluster [56].
The 60 % CS hybrid material also displays two C1s peaks at 284.8 and 287.8 eV, indicating a little difference in the binding energies compared with pure g-C3N4.
Two strong peaks at 464.3 and 458.6 eV are attributed to Ti 2p of TiO2 (Fig. 4c), which is slightly shifted toward lower binding energies compared with that of pristine TiO2 due to the direct contact between Ag nanoparticles and TiO2 [21].
Compound 11c possessed lower binding free energy compared with compounds 12a and 12c.
This binding energy was compared with the binding energy of influenza NP418 epitope to HLA B*3501 and found to be the same as the predicted epitope (−7.6 kcal/mol, Figure 2, A and B).
By docking studies and bioinformatic analyses, we show that ES indeed can bind to the ligand binding site of AR, with a considerable binding energy as compared with that of dihydrotestosterone, its natural ligand, reinforcing such a hypothesis.
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