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4 protocols using nicolet avatar 360 ft ir spectrophotometer

1

Characterization of GSH-Cu/Au Bionanoconjugates

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Fluorescence experiments were performed with a Hitachi F-4600 fluorescence spectrometer (Hitachi, Japan) with excitation at 380 nm and emission at 450 nm. Fourier transform infrared spectroscopy (FT-IR) spectra were recorded in the wavelength range of 4000–500 cm−1 with a Nicolet Avatar 360 FT-IR spectrophotometer (Thermo Fisher Scientific, USA). To study the morphology and estimate the mean diameter of the resultant GSH–Cu/Au BNCs, transmission electron microscopy (TEM) analyses were conducted on a JEOL-2100F transmission electron microscope (Japan) operating at an accelerating voltage of 200 kV. UltimaIV Powder X-ray diffraction (XRD) patterns were recorded using an X-ray diffractometer (Rigaku, Japan) operating at an accelerating voltage of 40 kV.
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2

Comprehensive Material Characterization Techniques

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Transmission electron microscopy (TEM) was performed using a JEM-2100F microscope (JEOL, Tokyo, Japan). Photoluminescence (PL) spectra were recorded on an RF-5301 PC spectrophotometer (Shimadzu Corp, Kyoto, Japan). Ultraviolet-visual light (UV-vis) absorption spectra were measured on a Shimadzu 3100 UV-Vis spectrophotometer. Fourier transform infrared (FT-IR) spectra were recorded on a Nicolet AVATAR 360 FTIR spectrophotometer (Thermo Fisher Scientific; Waltham, MA, United States). X-ray photoelectron spectroscopy (XPS) analysis was performed on an ESCALAB 250 spectrometer (Thermo Fisher Scientific) with a monochromatic Al Kα excitation source (1,486.6 eV).
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3

Characterization of N-Doped Graphene Quantum Dots

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The ultraviolet-visible
(UV–vis) absorption spectra and fluorescence spectrum were
recorded using a Hitachi U-2900 (Hitachi, Japan) UV–vis spectrophotometer
and a Hitachi F-4600 (Hitachi, Japan) fluorescence spectrophotometer,
respectively. The images of transmission electron microscopy (TEM)
were taken using a JEOL-2100F transmission electron microscope (Japan)
to probe the surface morphology and assess the average diameter of
N-GQDs. Fourier transform infrared (FT-IR) spectra were characterized
using a Nicolet Avatar 360 FT-IR spectrophotometer (Thermo Fisher
Scientific). X-ray diffraction patterns were measured using an X-ray
diffractometer (Rigaku, Japan). X-ray photoelectron spectroscopy (XPS)
data were collected by a Thermo Scientific ESCALab 250Xi. The fluorescence
lifetime was measured with an Edinburgh Instruments FLS980 fluorescence
spectrophotometer with excitation at 360 nm.
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4

Synthesis of Fmoc-Protected Peptides

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The preparation of Fmoc-FF-OFm, Fmoc-FFF-OFm and Fmoc-FFFF-OFm peptides was carried out following standard procedures of peptide synthesis in solution starting from the corresponding F-derivative and using the Boc or Fmoc group as protection for the amino moieties. A general procedure for the coupling reactions is given in Figure 1.
Melting points were determined on a Gallenkamp apparatus and are uncorrected. IR spectra were registered on a Thermo Nicolet Avatar 360 FTIR spectrophotometer;  max is given for the main absorption bands. 1 H and 13 C NMR spectra were recorded on a Bruker AV-400 or ARX-300 instrument at room temperature unless otherwise indicated and using the residual solvent signal as the internal standard; chemical shifts (δ) are expressed in ppm and coupling constants (J) in Hertz. Optical rotations were measured on a JASCO P-1020 polarimeter. High-resolution mass spectra were obtained on a Bruker Microtof-Q spectrometer.
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