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122 protocols using nicolet is50 spectrometer

1

FTIR Analysis of Irradiated Specimens

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Specimens for the FTIR study were analyzed after exposure to 70 Gy radiation (IR group) and the corresponding control treatment (C group). FTIR spectra were acquired using a Nicolet iS50 spectrometer (Thermo Fisher Scientific, Waltham, MA, USA) in a spectral range of 4000–400 cm−1 and a spectral resolution of 4 cm−1. The specimens were dried in a vacuum at room temperature for 7 days and fixed on an attenuated total reflectance (ATR) diamond crystal using a special press. The window of the ATR accessory sampled a circular area (d = 2.5 mm) from the center of each specimen. One spectrum per specimen was acquired by averaging 40 consecutive scans.
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2

Analyzing Protein Structure in Decellularized Samples

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The protein secondary structure of native and decellularized samples was studied using Fourier transform infrared spectroscopy (FTIR). NBPs, DBPs, NPPs, and DPPs flaps (10 × 10 mm2, n = 3 for each group) were cut and equilibrated for 3–4 h in deuterium oxide (Janssen, Beerse, Belgium) to reduce the contribution of interfering water bands in the amide-I region [42 (link)]. FTIR investigations were performed using the Nicolet iS-50 spectrometer (Thermo Fisher Scientific, Waltham, MA, USA) in the attenuated total reflectance (ATR) mode. The instrument was equipped with a diamond/ZnSe crystal and pressure arm. The transmittance of both samples and background was each measured using 64 scans and infrared spectra were collected within the 4000–500 cm−1 range, at room temperature. Spectra were then overlapped using a Matlab® script (Mathworks, Natick, MA, USA) [43 ] to compare the composition of the investigated materials. Amide-I and amide-II bonds, respectively at 1630 cm−1 and 1550 cm−1 [40 (link),43 ], were selected to evaluate the integrity of ECM proteins. Peak transmittance ratio (R) was calculated dividing the intensity of the amide-I peak by the intensity of the amide-II peak.
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3

FTIR Analysis of Control and Samples

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FTIR spectra of the control and obtained samples were recorded using a Nicolet iS50 spectrometer (Thermo Fisher Scientific Co., Hillsboro, OR, USA). Each measurement was performed using a built-in attenuated total reflectance (ATR) accessory. The analysis was carried out in the wavelength range of 4000–400 cm−1.
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Comprehensive Nanomaterial Characterization by TEM, FTIR, Raman, and XPS

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Transmission electron microscopy (TEM) images were acquired by Tecnai G2 F30 transmission electron microscope (FEI, Hillsboro, OR, United States). BP NSs were observed after being dropped onto a copper grid-coated carbon membrane and air-dried. Fourier transform infrared (FTIR) spectra were recorded with Nicolet iS 50 spectrometer (Thermo Scientific, United States). Raman spectra were recorded at room temperature by LabRAM HR800 high-resolution confocal Raman microscope (HORIBA, United States). X-ray photoelectron spectroscopy was performed with Axis HSi X-ray photoelectron spectroscope (Kratos Ltd., United Kingdom) employing Al Kα radiation (150 W, 1486.6 eV photons) as the excitation source. Zeta potential and size were measured by Malvern Mastersizer 2000 particle size analyzer (Zetasizer Nano ZS90, Malvern Instruments Ltd., United Kingdom). All measurements were conducted three times independently and averaged.
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5

Probing Rhombohedral BiFeO3 by FTIR and AFM-IR

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To have a first glimpse of the IR absorption for rhombohedral BiFeO3, FTIR was carried out based on a Nicolet iS50 spectrometer (Thermo Fisher) under grazing incidence mode with IR beam polarized vertical to the substrate plane. Accordingly, we observed strong absorption at ~500 cm−1, for the rhombohedral continuous thin film. To further distinguish the IR absorption for rhombohedral BiFeO3 nanocrystals with upward, downward quad-domains and the Solomon topological polar structure, AFM-IR with an ultra-high spatial resolution is carried out as shown in Fig. 4 in the main text.
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6

FT-IR Spectroscopy of Powdered Samples

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Prior to measurements, powders were blended with dried KBr particles (95 °C, 4 h) and pressed as transparent pellets. Spectra were obtained with a Thermo Fisher Nicolet iS50 spectrometer in transmission mode from 400 to 4000 cm−1 with a spectral resolution of 4 cm−1, with 16 scans per spectrum.
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7

Characterization of Pt-Ni Nanoparticles

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TEM images were conducted
on a FEI Tecnai G2 spirit operated at an accelerating voltage
of 120 kV. The real metal loading and composition of the Pt–Ni
NPs was measured by ICP optical emission spectrometry (ARCOS II MV
SPECTRO). XRD patterns were collected on a D8 ADVANCE-diffractometer
(Bruker) equipped with a LynxEye detector and KFL Cu 2K X-ray tube.
UV/vis spectroscopy was carried out on an Agilent Cary 5000 spectrometer.
The FTIR spectra were measured on a Thermo Scientific Nicolet iS50
spectrometer by placing a few drops of the solution on the surface
of a diamond cell.
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8

FTIR Characterization of Porcine SIS Tissue

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Native (n = 3) and decellularized (n = 3) porcine SIS tissues were processed for Fourier transform infrared spectroscopy (FTIR) using a Nicolet iS-50 spectrometer (Thermo Fisher Scientific, Waltham, MA, USA) with an Attenuated Total Reflectance (ATR) accessory. The instrument was equipped with diamond/ZnSe crystal and pressure arm. Infrared spectra of the samples and background were collected using 64 scans in the range of 4000-500 cm−1 to characterize the composition of each group of samples.
Data were analysed using a Matlab® script (Mathworks, Natick, MA, USA) [108 ].
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9

Characterization of H2L Ligand Synthesis

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The ligand H2L was synthesized according to the literature method.30 All of the other reagents and chemicals were of an analytical grade and obtained from commercial sources. Powder X-ray diffraction (PXRD) data were collected on a PANalytical X’Pert PRO MPD system (PW3040/60). Fourier transform infrared (FT-IR) measurements were conducted on a Thermo Nicolet iS50 spectrometer. Scanning electron microscopy (SEM) images were taken on a Hitachi SU8010 instrument. X-ray photoelectron spectroscopy (XPS) data were obtained with a Thermo Escalab 250 spectrometer with monochromated Al-Kα excitation. The zeta potentials were determined using dynamic light scattering (DLS) on a Malvern Instruments Nanosizer-ZS. Thermogravimetric analysis (TGA) was carried out on a Netzsch STA-449F3 thermogravimetric analyzer under a nitrogen atmosphere at a heating rate of 10 °C min–1. Simultaneous inductively coupled plasma optical emission spectrometry (ICP-OES) on a PerkinElmer Optima 8000 instrument was used to determine the metal ion concentration in aqueous solution.
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10

Characterizing Chemical Bonds in e-HMs

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Chemical bonds in e-HMs were studied by Fourier transformed infrared spectroscopy (FTIR) in attenuated total reflectance mode (ATR). Acquisition was performed in the range 4000–400 cm−1, with resolution of 4 cm−1, for 64 scans. These analyses were performed with a Nicolet iS50 spectrometer by Thermo Scientific (Waltham, MA, USA).
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