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Spectrum 100 atr ftir spectrometer

Manufactured by PerkinElmer
Sourced in United States

The Spectrum 100 ATR-FTIR Spectrometer is an analytical instrument designed for Fourier-transform infrared (FTIR) spectroscopy. It utilizes attenuated total reflection (ATR) technology to analyze the chemical composition of solid, liquid, and semi-solid samples. The Spectrum 100 ATR-FTIR Spectrometer provides quantitative and qualitative data about the molecular structure and functional groups present in the sample.

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9 protocols using spectrum 100 atr ftir spectrometer

1

Deuteration Quantification via FTIR-ATR

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Fourier-transform infrared spectroscopy spectra of the chemically deuterated fibers were recorded with a PerkinElmer Spectrum 100 FTIR-ATR spectrometer (Waltham, MA, USA). The spectra in the wavelength range of 800–4,000 cm−1 were collected with a resolution of 2 cm−1 and a scan number of 64. The deuteration level of the fibers was calculated by the peak intensity ratio of OH/(OH+OD) after baseline correction, as previously reported (Song et al., 2020 (link)).
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2

FTIR Analysis of API and Excipients

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Infrared absorption spectra of API, excipients and 1:1 w/w physical mixtures of API and excipient were generated using a Spectrum 100 FTIR ATR spectrometer (Perkin Elmer®, Beaconsfield, UK). A small amount of each sample was placed onto a diamond crystal and subjected to a force of approximately 100 N prior to analysis at a rate of 4 cm−1 (n = 6 scans) over the wavelength range of 650–4000 cm−1. The data were analysed using Peak® version 4.00 spectroscopy software (Operant LLC, Burke, VA, USA).
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3

ATR-FTIR Analysis of Irradiated Membranes

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FTIR of the samples were collected using ATR technique. The equipment used was Perkin-Elmer Spectrum 100 ATR-FTIR Spectrometer. For irradiated sample, the mixed matrix membranes sample were first irradiated for about 5 minutes using Omnicure S1500 and then immediately followed by measuring the spectrum.
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4

Characterization of Ligand Purity

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Purity of the ligand was evaluated by using Bruker nuclear magnetic resonance (NMR) spectroscopy. Proton and carbon NMR spectroscopy was recorded using 400 and 101 MHz instrument, respectively, and using d6-DMSO as the solvent.
PXRD spectrum was collected using PANalytical X-Ray Diffractometer Instrument. The power of the instrument was set to 40 kV and 20 mA. Copper Kα was used as the X-ray source.
FTIR spectrum was collected using Perkin-Elmer Spectrum 100 ATR-FTIR Spectrometer. For after-UV light experiment, the sample was first irradiated with the Omnicure S1500 for about 5 minutes. This was then quickly followed by pressing to the ATR-FTIR equipment and FTIR spectrum was collected.
UV-Vis spectrum of the free ligand was collected using Thermo Scientific NanoDrop 2000 Spectrophotometer. The ligand was dissolved in dimethylsulfoxide (DMSO) before the measurement. The ligand solution was then irradiated using a 365 nm UV light LED purchased from Thorlab (3.65 V; 1.1 Amp) for 40 min before the after-UV measurement took place.
CCDC number for JUC-62 is 666395. Figure 1(a) in the manuscript is generated by using Mercury software.
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5

FTIR Analysis of Lyophilized Samples

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Prior to FTIR analysis, samples were washed once following the same protocol as noted for the SEM preparations and frozen at −20 °C overnight. The frozen samples were then lyophilized using a Labconco lyophilizer (Labconco, Kansas City, MO, USA) to obtain a dry powder for further analysis. The FTIR spectra of samples were recorded using a Perkin Elmer Spectrum 100 ATR FTIR Spectrometer (PerkinElmer, Waltham, MA, USA).
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6

Characterization of Chitosan-Manganese Vesicles

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Prior to FTIR studies, the samples were frozen and lyophilized (FreeZone 4.5 L Freeze Dry System, Labconco, Kansas City, MO, USA) to obtain a dry powder for further analysis. To demonstrate the presence of Mn ions within the chitosan vesicles (Chi), the FTIR spectra of powder Chi-Mn and corresponding controls (MnAc and Chi) were recorded using a Perkin Elmer Spectrum 100 ATR FTIR Spectrometer (PerkinElmer, Waltham, MA, USA).
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7

Comprehensive Polymer Film Characterization

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CV characterizations of polymer films were performed on the same Autolab PGstat12 Potentiostat/Galvanostat. The tests were performed in 1× monomer-free phosphate buffered saline (PBS) solution with an Ag/AgCl glass body electrode (Thermo Fisher Scientific) as the reference. The scan rate was 100 mV/s.
EIS was performed in an electrochemical cell installed with a platinum foil as the counter electrode. Monomer-free PBS was used as the electrolyte. The same Autolab was used. For EIS measurement, a bias of 0.01 V versus Ag/AgCl was applied. The frequency range between 1 and 100 kHz was scanned. Attenuated total reflectance FTIR (ATR-FTIR) spectroscopy was performed on a PerkinElmer Spectrum 100 ATR-FTIR spectrometer. UV-vis-NIR spectra were collected on a Shimadzu UV-3600 UV-VIS-NIR spectrophotometer.
FIB-SEM was performed on an Auriga 60 CrossBeam FIB-SEM (Carl Zeiss). For SEM imaging, an acceleration voltage of 3 kV was used. For FIB milling, a 20-pA gallium ion beam was applied.
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8

Maillard Conjugation of BSA and SF20

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Maillard reaction was used to conjugate BSA and SF20 using a molar ratio of 1:1, lysine residues of BSA: SF20 [30] (link). Both BSA and SF20 were dissolved together in 10 mM phosphate buffer and the pH of the mixture was adjusted to pH 8.0 using NaOH. The mixture was then stirred at 500 rpm for 12 h in the dark at room temperature. The resultant dispersion was lyophilized and then reacted inside a desiccator pre-conditioned using a saturated solution of KBr to yield 79 % relative humidity at 60 °C. This BSA + SF20 Maillard copolymer conjugate was denoted as BSMcon henceforth. The conjugation degree of the conjugate was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) at a protein load of 10 µg well -1 and O-phthaldialdehyde (OPA) assay as described elsewhere [31] (link).
Additionally, Fourier transform infrared (FTIR) spectra (4500 -400 cm -1 , where 32 scans were averaged with a resolution of 2 cm -1 ) of the conjugates were obtained. Samples were prepared as KBr pellets and scanned against air background on a Spectrum 100 ATR-FTIR Spectrometer (Perkin Elmer Inc., USA) with KBr correction optics.
Control groups included BSA + ACS Maillard copolymer conjugate (BAMcon) without any addition of folic acid groups produced under the same reaction conditions and native bovine serum albumin (BSAnative) protein.
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9

Physicochemical Characterization of [P4444][Ph-tet]

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Microanalyses and electrospray MS were performed by ASEP, Queen's University Belfast.. 1 H, 13 C and 31 P NMR spectroscopy in DMSO-d 6 using a Bruker Avance III 400 MHz spectrometer. FT-IR spectra were performed using a PerkinElmer Spectrum 100 ATR FT-IR spectrometer. The melting point for the pure [P 4444 ][Ph-tet] was determined by differential scanning calorimetry (TA DSC Q2000 with a refrigerated cooling system, 5-20 mg samples, 1 °C min -1 heating and cooling rates under dinitrogen, scanning between -100 and +100 °C or between -15 and 25 °C). The decomposition temperature of [P 4444 ][Ph-tet] was measured in the dynamic heating regime using a TA Instruments Q5000 TGA instrument under nitrogen atmosphere. Samples were heated from room temperature to 500 °C under constant heating rate of 10 °C min -1 .
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