Following the synthesis, the nanoliposomes were diluted 1:5000 and 1:10 for nanoparticle tracking analysis (NTA) and dynamic light scattering (DLS), respectively. NTA measurements were recorded and analyzed using the Nanosight NS300 (Malvern, UK); DLS and Zeta potential measurements were performed using the Brookhaven Zeta-PALS light-scattering analyzer (New York, NY, USA). Fourier-transform infrared spectroscopy was performed using the Perkin Elmer FTIR Spectrum II (Waltham, MA, USA) on lyophilized samples. Absorbance measurements were performed in 96-well plates at various dilutions using the Spectramax i3 (Molecular Devices, San Jose, CA, USA). For transmission electron microscopy, immediately after synthesis, liposomes were drop cast on a carbon-copper grid and stained with uranyl acetate for contrast. The imaging was performed using the FEI Tecnai G2 Spirit Twin TEM (Hillsboro, OR, USA) at a voltage of 120 kV.
Ftir spectrum 2
Manufactured by PerkinElmer
Sourced in United States
The PerkinElmer Spectrum-2 FTIR (Fourier Transform Infrared) spectrometer is a laboratory instrument used for the analysis of molecular structures. It measures the absorption of infrared radiation by a sample, generating a spectrum that can be used to identify and characterize various chemical compounds.
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Lab products found in correlation
Tecnai g2 spirit twin tem, by Thermo Fisher Scientific (1 mentions)
Spectramax i3, by Molecular Devices (1 mentions)
Pregnenolone, by Merck Group (1 mentions)
Pregnenolone sulphate, by Merck Group (1 mentions)
P 200 polarimeter, by Jasco (1 mentions)
6520 accurate mass q tof, by Agilent Technologies (1 mentions)
Bovine serum albumin (bsa), by Merck Group (1 mentions)
Lambda 750 spectrophotometer, by PerkinElmer (1 mentions)
Tecnai g2 20s twin transmission electron microscope, by Thermo Fisher Scientific (1 mentions)
X pert pro diffractometer, by Malvern Panalytical (1 mentions)
Ls 55 fluorescence spectrometer, by PerkinElmer (1 mentions)
Jsm 6490la, by JEOL (1 mentions)
X maxn sdd 50 mm2 edxs detector, by Oxford Instruments (1 mentions)
Evo hd15, by Zeiss (1 mentions)
10 protocols using ftir spectrum 2
1
Nanoliposome Characterization and Analysis
2
FTIR Analysis of Hydrogel Spectra
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The spectra of the different hydrogels were obtained using an FTIR Spectrum II (Perkin Elmer, Waltham, Massachusetts, USA) with ATR. The data were normalized to the background spectrum without a hydrogel. Next, the hydrogels were clamped down and a spectral range of 400–4000 cm-1 was recorded with four scans and a resolution of 1 cm-1.
3
Analytical Characterization of Compounds
4
Optical Properties of Graphene Quantum Dots
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FTIR, Raman, UV–vis, and fluorescence spectroscopy measurements were carried out to determine the optical properties of GQDs. A Perkin Elmer LAMBDA 750 spectrophotometer was used to record the UV–visible absorbance spectrum. The luminescence characteristics of the GQDs were investigated using a Perkin Elmer LS 55 fluorescence spectrometer. On a Perkin Elmer FT-IR Spectrum 2, FTIR spectra were measured in the range of 500–4000 cm−1 by making KBr pellets of the sample. At room temperature, an AIRIX STR 500 laser Raman spectrometer was used with Ar laser excitation at 532 nm. A Panalytical X-Pert Pro diffractometer with Cu Kα radiation (λ = 1.5418 Å) was used for investigating the structural properties of GQDs. Morphology and size of GQDs were confirmed with data obtained from a Bruker AFM analyzer atomic force microscope and a FEI Tecnai G2 20 S-TWIN transmission electron microscope.
5
Characterization of Biofilm Matrices
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Fourier transform infrared (FTIR) spectroscopy, scanning electron microscopy (SEM), and Congo red and Calcofluor binding assays were used to identify the components of the biofilm matrices, i.e., EPS. For the FTIR analysis, the pellets were prepared as described in Mosharaf et al. (2018) (link). Using the triglycine sulfate (TGS) detector, 450 to 4000 cm–1 was scanned (16 scans at 4 cm–1 resolution and at 0.2 cm sec–1 scanning speed). The IR spectra of the biofilm matrices were acquired using the Perkin Elmer FTIR (Spectrum-2) instrument operated by CPU32M software. Perkin Elmer’s proprietary software (Version 10.05.03) was used to analyze the baseline subtracted biofilm spectra. For SEM, 72-hour-old biofilms were carefully collected and then oven dried at 40°C for 48 h. Each dried sample was coated with carbon using a vacuum sputter-coater to improve the conductivity. A scanning electron microscope (SEM, JEOL JSM-6490LA, Japan) operated at 5.0 KV was used to image the samples. To detect curli fimbriae and nanocellulose, Congo red and Calcofluor binding assays were performed as described in Haque et al. (2009 (link), 2017) (link).
6
FTIR Analysis of Metabolite Preparations
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The metabolites were prepared as described in earlier section. FTIR analysis was carried out using Perkin Elmer FTIR (Spectrum-2) instrument operated by CPU32M software. Triglycine sulphate (TGS) detector was applied for FTIR scanning within 600 to 2000 cm−1 (16 scans at 4 cm−1 at 0.2 cm/sec scanning speed) and changes in the percent transmission at different wavenumbers were recorded. YEP without MO was also scanned. Perkin Elmer’s proprietary software (Version 10.05.03) was used to analyze the baseline subtracted spectra.
7
FTIR Analysis of Powder Samples
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The samples were analyzed in the scanning range of 4000 cm−1~400 cm−1 and a resolution of 2 cm−1 by PerkinElmer FTIR spectrum 2 (Liantrisant, UK). Before testing, the samples were treated with potassium bromide at a ratio of 1:100, and then the powder mixtures were compressed into tablets at a pressure of 30 MPa. The background was scanned first before scanning the samples [77 (link)].
8
Characterization of Materials via Spectroscopic Techniques
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Infrared (IR)
spectra were recorded on a Perkin Elmer Spectrum 2 FT-IR instrument
(optical resolution of 0.5 cm–1) in attenuated total
reflectance (ATR) measurement mode (analyses in the 400–4000
cm–1 range, performed by averaging four acquisitions
per sample).
pXRD analyses were performed on an X’Pert
MPD diffractometer using Cu Kα1 radiation (λ
= 1.5406 Å) with the operating voltage and current maintained
at 40 kV and 25 mA, respectively. Diffractograms were recorded between
5 and 60° in 2θ, with a step size of 0.017° (with
a count time per step of ∼50 s).
SEM analyses were carried
out on a Zeiss Evo HD15 scanning electron
microscope equipped with an Oxford Instruments X-MaxN SDD 50 mm2 EDXS detector. Before the SEM analyses, samples were deposited
on a double-sided conducting carbon tape and then metallized with
carbon.
spectra were recorded on a Perkin Elmer Spectrum 2 FT-IR instrument
(optical resolution of 0.5 cm–1) in attenuated total
reflectance (ATR) measurement mode (analyses in the 400–4000
cm–1 range, performed by averaging four acquisitions
per sample).
pXRD analyses were performed on an X’Pert
MPD diffractometer using Cu Kα1 radiation (λ
= 1.5406 Å) with the operating voltage and current maintained
at 40 kV and 25 mA, respectively. Diffractograms were recorded between
5 and 60° in 2θ, with a step size of 0.017° (with
a count time per step of ∼50 s).
SEM analyses were carried
out on a Zeiss Evo HD15 scanning electron
microscope equipped with an Oxford Instruments X-MaxN SDD 50 mm2 EDXS detector. Before the SEM analyses, samples were deposited
on a double-sided conducting carbon tape and then metallized with
carbon.
9
RITC-RGD:PB Particle Conjugation
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RGD peptide and PBNPs were combined in a 1:200 (peptide:nanoparticle)
volumetric ratio in 4 mM borate buffer as previously reported with
a similar method.68 (link) The solution was left
to mix overnight at RT. The following day, the particle mixture was
washed at 12 000 rpm for 30 min (×2) with DDI water. Final
RITC-RGD:PB particles are stored in water. Conjugation was validated
using a PerkinElmer Spectrum 2 FTIR through a drop cast method.
volumetric ratio in 4 mM borate buffer as previously reported with
a similar method.68 (link) The solution was left
to mix overnight at RT. The following day, the particle mixture was
washed at 12 000 rpm for 30 min (×2) with DDI water. Final
RITC-RGD:PB particles are stored in water. Conjugation was validated
using a PerkinElmer Spectrum 2 FTIR through a drop cast method.
10
PEGylated Prussian Blue Nanoparticle Synthesis
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PEGylated
Prussian Blue nanoparticles (PEG:PB) were prepared via a two-step
synthesis with some modifications.67 (link) Initially,
PBNPs were synthesized to include a PVP coating using a coprecipitation
reaction. Iron(III) chloride (1 mM) is mixed with potassium hexacyanoferrate
(II) trihydrate (1 mM) while in the presence of PVP and stirred at
60 °C overnight. The next day, the reaction mixture was washed
with a 1:1 water and acetone mixture at 12,000 rpm for 20 min (×3).
Particles were then PEGylated by doing a surfactant substitution.
PVP–PBNP (2 mg/mL) was mixed with an equal amount of poly bis(amine)
and stirred at RT for 24 h. The next day, the PEG:PB particles were
washed with DDI water (×3). Final solution was suspended in water.
Conjugation was validated using a PerkinElmer Spectrum 2 FTIR through
a drop cast method.
Prussian Blue nanoparticles (PEG:PB) were prepared via a two-step
synthesis with some modifications.67 (link) Initially,
PBNPs were synthesized to include a PVP coating using a coprecipitation
reaction. Iron(III) chloride (1 mM) is mixed with potassium hexacyanoferrate
(II) trihydrate (1 mM) while in the presence of PVP and stirred at
60 °C overnight. The next day, the reaction mixture was washed
with a 1:1 water and acetone mixture at 12,000 rpm for 20 min (×3).
Particles were then PEGylated by doing a surfactant substitution.
PVP–PBNP (2 mg/mL) was mixed with an equal amount of poly bis(amine)
and stirred at RT for 24 h. The next day, the PEG:PB particles were
washed with DDI water (×3). Final solution was suspended in water.
Conjugation was validated using a PerkinElmer Spectrum 2 FTIR through
a drop cast method.
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