The CL spectra were recorded using a BPCL ultra-weak luminescence analyzer (Institute of Biophysics, Chinese Academy of Sciences, Beijing, China) with the condition of a photomultiplier tube voltage of -850 V. The CL spectra of the relationship between the wavelength and the intensity were captured by closing the excitation slit on the F-2700 spectrofluorometer (Hitachi, Japan). The absorption spectra were recorded with a UV-3100 UV-VISNIR spectrophotometer (Shimadzu, Japan). X-ray photoelectron spectroscopy (XPS) was performed using an ESCALAB 250 spectrometer. Transmission electron microscopy (TEM) images were obtained using a FEI Tecnai G2 S-Twin instrument under an accelerating voltage of 200 kV. Energy diffraction X-ray (EDX) spectra were obtained by TEM.
F 2700 spectrofluorometer
Manufactured by Hitachi
Sourced in Japan
The F-2700 spectrofluorometer is a laboratory instrument designed for the detection and analysis of fluorescent compounds. It measures the intensity of fluorescence emitted by a sample when exposed to a specific wavelength of light. The instrument provides accurate and reliable data for various applications in fields such as biochemistry, materials science, and environmental analysis.
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Lab products found in correlation
Uv 3100 uv visnir spectrophotometer, by Shimadzu (2 mentions)
Jem 2100, by JEOL (1 mentions)
Lambda 35, by PerkinElmer (1 mentions)
J 1500, by Jasco (1 mentions)
Autoflex 3, by Bruker (1 mentions)
Afm5500m, by Hitachi (1 mentions)
Fls980 spectrometer, by Edinburgh Instruments (1 mentions)
Dsc q200, by TA Instruments (1 mentions)
Ftir spectrophotometer, by PerkinElmer (1 mentions)
10 protocols using f 2700 spectrofluorometer
1
Nanomaterial Characterization Protocol
2
Multimodal Characterization of Materials
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A BPCL ultra-weak luminescence analyzer (Institute of Biophysics, Chinese Academy of Sciences, Beijing, China) with a photomultiplier voltage of -850 V was used to investigate the CL experiment in the whole process. Fluorescence spectra were captured by closing the excitation slit on the F-2700 spectrofluorometer (Hitachi, Japan). The UV-3100 UV-VISNIR spectrophotometer (Shimadzu, Japan) was applied to acquire data of the absorption spectra. Infrared spectra were recorded as KBr disks with an Avatar 360 (Nicolet, USA) spectrometer. X-ray photoelectron spectroscopy (XPS) was performed using an ESCALAB 250 spectrometer. The 1 H NMR spectrum was obtained under a Varian Mercury YH-300 spectrometer operated at 400 MHz.
3
Protein Surface Hydrophobicity Assay
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Protein surface hydrophobicity (H0) was determined using the ANS probe assay [22 (link)]. All ANS (8 mM) and protein samples (0.2–1 mg/mL) were prepared in pH 7.0 phosphate buffer (10 mM). The 4 mL protein samples were thoroughly mixed with 20 μL ANS. After 3 min of reaction in the dark, the fluorescence intensity was measured using an F-2700 spectrofluorometer (Hitachi, Tokyo, Japan) under the conditions described below. Excitation wavelength: 390 nm; emission wavelength: 470 nm; slit width: 5 nm. The standard curve was plotted with the protein concentration (mg/mL) of samples as the abscissa and the fluorescence as the ordinate, and the slope of the curve was determined as H0.
4
Fluorometric Analysis of DNA-Protein Interaction
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The interactions between the DNA with protein in the absence or presence of Tb3+ were measured using a HITACHI F-2700 spectrofluorometer. For the affinity of DNA towards protein (10 μM), the excitation wavelength was set at 280 nm. Titration was carried out with increasing concentrations of DNA (0–20 μM) to the protein of HsCen2 or HsCen2p, and the corresponding emission spectra were recorded. To detect the effect of Tb3+ on DNA binding to protein, protein (10 μM) was incubated with Tb3+ 1 : 2 for 10 min at 4 °C, and the Tb2-protein was titrated by gradually increasing the DNA concentration from 0 to 10 μM. The excitation wavelength was set to 295 nm, and the scanning range was 310–500 nm. Both the slit widths for excitation and emission were 10 nm. The reported constants are averages of three experiments.
Binding of the protein (HsCen2 or HsCen2p or Tb2-HsCen2 or Tb2-HsCen2p) with 2-p-toluidinylnaphthalene-6-sulfonate (TNS) was monitored by a fluorescence spectrometer. After incubation of the proteins with TNS for 10 min at 4 °C in the absence or presence of DNA, the mixed solutions were excited at 320 nm, and the scanning range was 330–650 nm.
Binding of the protein (HsCen2 or HsCen2p or Tb2-HsCen2 or Tb2-HsCen2p) with 2-p-toluidinylnaphthalene-6-sulfonate (TNS) was monitored by a fluorescence spectrometer. After incubation of the proteins with TNS for 10 min at 4 °C in the absence or presence of DNA, the mixed solutions were excited at 320 nm, and the scanning range was 330–650 nm.
5
Fluorescence Spectroscopy of SG-CB[n] Interactions
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Fluorescence spectra were acquired with a F-2700 spectrofluorometer (Hitachi High-Technology Corp, Japan). The fluorescence was measured in a quartz cell with a path length of 1 cm under excitation at 327 nm. SG at the specified concentration was added into the solution buffered with 50 mM PBS (0.1 M K + ) at the specified pH, and the resulting solutions were allowed to incubate for 30 min before the addition of CB [n]. Fluorescence measurements were measured at 20°C after incubating the resultant solution with HSO3 -or other species for 30 min.
6
Characterization of Fluorescent Carbon Dots
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The molecular weight of FCDs was measured by matrix-assisted laser desorption/ionization time-of-flight mass spectrometer (MALDI-TOF-MS, Autoflex III, Bruker Daltonics, Bremen, Germany), using 2, 5-dihydroxybenzoic acid as a matrix. Transmission electron microscope (TEM) analysis was used a TEM (JEM-2100, JEOL, Tokyo, Japan) at a voltage of 200 kV. The ultrasonic particle size analyzer (DT1200) was used to measure the ζ-potential of the samples. UV-Vis spectrophotometer (Lambda 35, PerkinElmer, Norwalk, CT, USA) was used to record the absorption spectra. The fluorescence spectra were performed with the F-2700 spectrofluorometer (Hitachi, Tokyo, Japan). The fluorescence lifetime was ascertained by an FLS980 spectrometer (Edinburgh Instruments, Edinburgh, UK). FTIR was conducted by a PerkinElmer spectrometer (Frontier, Norwalk, CT, USA). CD spectra were performed by a JASCO circular dichroism spectrometer (J-1500, Tokyo, Japan). Atomic force microscope (AFM) was used to measure the two/three-dimensional morphology and height of the samples (AFM-5500M, Hitachi, Tokyo, Japan). Unless otherwise stated, the sample concentration was 1 mg/mL. All samples were dissolved in PBS buffer (0.01 M, pH 7.2–7.4). Before the test, the FCDs and protein mixture liquid was incubated in a water bath at 37 °C for 10 min.
7
Fluorometric Enzyme Inhibition Assays
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The screening assays for the inhibitory activity of the compounds in the rCPB2.8, rCPB3, and rH84Y enzymes were performed using 100 mM sodium acetate buffer containing 5 mM EDTA, 100 mM NaCl, 0.01% Triton X-100, and 20% glycerol, at pH 5.5. Enzyme aliquots were pre-incubated with 5 mM DTT for 5 min at 37 °C. After checking the initial rate of the reaction corresponding to the control, the enzymatic rate was measured at two concentrations of compounds, 1 µM and 5 µM. Enzyme activity was monitored by hydrolysis of the substrate Z-FR-MCA by measuring the fluorescence at λEx = 360 nm and λEm = 480 nm on a Hitachi F2700 spectrofluorometer, obtaining the rate values in UAF/min (arbitrary fluorescence units by minute).
8
Physico-chemical Characterization of Inclusion Complexes
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Ultraviolet–visible (UV–Vis) and fluorescence spectral measurements were performed using a UV 3220 spectrometer (Optizen, Redmond, WA, USA) and F-2700 spectrofluorometer (Hitachi, Tokyo, Japan). Fourier-transform infrared spectroscopy (FTIR) was performed using an FTIR spectrophotometer (Perkin Elmer, Waltham, MA, USA) at a scanning range of 4000–400 cm−1. The powder X-ray diffractometry (XRD) patterns for AVR, Mβ-CD, and Mβ-CD:AVR inclusion complexes were obtained using an X-ray diffractometer (PANalytical X’Pert Philips, MRD model; Malvern Panalytical, Malvern, UK) at a voltage and current of 40 kV and 30 mA, respectively (wavelength: 1.5405 Å scanning speed; 5° min−1, range; 10–80°). Thermogravimetric analysis (TGA) and differential scanning calorimetry (DSC) analysis of β-CD and the Mβ-CD:AVR inclusion complex (temperature range: 25–400 °C and heating rate: 10 °C min−1 under nitrogen) was performed using a TGA-Q5000 thermal analyzer (TA Instruments, New Castle, DE, USA) and DSC Q200 (TA Instruments). The surface morphologies of AVR, Mβ-CD, and Mβ-CD:AVR inclusion complexes were examined by scanning electron microscopy (SEM) with a FESEM Leo Supra 50VP (Carl Zeiss SMT, Oberkochen, Germany) microscope at an accelerating voltage of 200 kV. All the samples were immobilized on double-sided carbon tape without further coating as the extent of sample preparation.
9
Protein Surface Hydrophobicity Measurement
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ANS was used as a fluorescent probe to determine the S0 values of proteins. The protein samples were firstly configured with 0.01 mol/L phosphate buffer (pH 7.0) to a series of concentrations of 0.2, 0.4, 0.6, 0.8 and 1 mg/mL and then 20 μL of 8 mmol/L ANS solution was added to 4 mL of the above concentrations of protein solution, shaken well and left for 3 min, and then the fluorescence intensity was recorded at an excitation wavelength of 390 nm and an emission wavelength of 470 nm by using an F-2700 spectrofluorometer (Hitachi, Japan). The slope of the curve is the surface hydrophobicity value of the protein.
10
UV-Vis and Tryptophan Fluorescence Analysis
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Ultraviolet absorption spectroscopy: The ultraviolet spectra of native and modified protein samples (150 µg/mL) were estimated within the wavelength range of 200–420 nm on a UV–spectrophotometer.
Tryptophan fluorescence spectroscopy: The fluorescence of tryptophan residues in native and modified protein samples was estimated at an excitation wavelength of 285 nm. The emission for all of the samples was recorded over the range of 290 to 440 nm [38 (link)]. For the analysis, the concentration of protein samples was 100 mM. All readings were measured on a Hitachi model F2700 spectrofluorometer (Japan).
Tryptophan fluorescence spectroscopy: The fluorescence of tryptophan residues in native and modified protein samples was estimated at an excitation wavelength of 285 nm. The emission for all of the samples was recorded over the range of 290 to 440 nm [38 (link)]. For the analysis, the concentration of protein samples was 100 mM. All readings were measured on a Hitachi model F2700 spectrofluorometer (Japan).
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