The attenuated total reflectance Fourier transform infrared (ATR-FTIR) analyses of gelatins (BBG and OBBG) were performed according to our previous work (Zhang, Sun, et al., 2020 ). Briefly, freeze-dried gelatins were examined by an ATR-FTIR spectrometer (Spotlight 400, PerkinElmer, Waltham, Massachusetts, USA) with a wavenumber range of 500–4000 cm−1. The areas of 1700–1600 cm−1 were used to analyze the secondary structure percentages of gelatins by PeakFit software (V4.12, SeaSolve, Framigham, MA, USA) (Xu et al., 2021 (link)).
Spotlight 400
Manufactured by PerkinElmer
Sourced in United States, France, United Kingdom
The Spotlight 400 is a Fourier transform infrared (FTIR) imaging spectrometer designed for chemical and molecular analysis. It features a high-sensitivity mercury cadmium telluride (MCT) detector and advanced optics to enable rapid, high-resolution infrared imaging.
Automatically generated - may contain errors
Lab products found in correlation
Spectrum 400, by PerkinElmer (2 mentions)
Frontier ft ir spectrometer, by PerkinElmer (2 mentions)
Spectrum 100 optica, by PerkinElmer (1 mentions)
Su8220, by Hitachi (1 mentions)
Opus 7, by Bruker (1 mentions)
Matlab 2014b, by MathWorks (1 mentions)
Human mao b, by Merck Group (1 mentions)
Avance 3 spectrometer, by Bruker (1 mentions)
Flash 2000 chns o analyzer, by Thermo Fisher Scientific (1 mentions)
Recombinant human mao a, by Merck Group (1 mentions)
Quanta 200 feg, by Thermo Fisher Scientific (1 mentions)
Isys software, by Malvern Panalytical (1 mentions)
Nicolet is10, by PerkinElmer (1 mentions)
3532 50 lcr hitester, by HIOKI (1 mentions)
Spectrum 400 ftir spectrophotometer, by PerkinElmer (1 mentions)
Model s 4800, by Hitachi (1 mentions)
Model s9i, by Leica (1 mentions)
Nicolet is5, by Thermo Fisher Scientific (1 mentions)
Spectrum 2, by PerkinElmer (1 mentions)
Hyaluronidase, by Merck Group (1 mentions)
50 protocols using spotlight 400
1
ATR-FTIR Analysis of Gelatin Structures
2
FTIR Imaging of Prostate Tissue
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IR images were acquired using a Spotlight 400 (Perkin Elmer) IR imaging instrument at a spatial pixel size of 6.25 µm × 6.25 µm and a spectral resolution of 4 cm−1 at an under-sampling ratio of 2. The spectral profile of a pixel was truncated to a spectral range of 4000–720 cm−1 for ease of data handling and classification. The sample was imaged in the reflection–absorption mode. Data were water vapor corrected and used for classification using the previously described Bayesian approach, metrics, and algorithms for prostate tissue. Further details of FTIR spectroscopy is provided in Supplementary Note 1 .
3
Bone Sample NIR Spectral Imaging
4
FTIR Analysis of Protein Film Structure
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Samples were dried into films at 40 °C and then investigated using a Perkin-Elmer Spotlight 400 Fourier transform infrared (FTIR) imaging system equipped with a germanium attenuated total reflection (ATR) crystal. IR absorption spectra were recorded in ATR image mode for the region between 750 cm−1 and 4000 cm−1 with 16 scans and a resolution of 4 cm−1. FTIR spectra were deconvoluted into 9 Gaussian peaks in the amide I band (1580 cm−1 to 1700 cm−1) using fixed peak positions, an enhancement factor (γ) of 2 and a smoothing filter of 70%. The procedure and peak positions/assignments were the same as those used by Cho et al.28 (link)
5
Gelatin-β-CD Characterization by ATR-FTIR
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The characterized spectra of gelatins with β-CD were studied using attenuated total reflectance Fourier transform infrared (ATR-FTIR) spectrometry (26 (link)). After the deodorization process (section 2.3), the deodorized gelatin solutions (66.7 mg/mL) with β-CD (30 mg/mL) were freeze-dried to obtain dried samples. The freeze-dried samples were examined using an ATR-FTIR spectrometer (Spotlight 400, PerkinElmer, Waltham, MA, United States) with a range of 600–4,000 cm−1, an average scan of 32, and a resolution of 1 cm−1.
6
Infrared Spectroscopy of Specimens
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Infrared spectra were collected using a Perkin-Elmer Spotlight 400 instrument with 4 cm−1 resolution. All spectra were background subtracted and specimens required no further preparation.
7
Bone Tissue Analysis by FT-IR Spectroscopy
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Tibiae of male mice were fixed in 70% EtOH and embedded in Osteoresin, and sections (4 μm in thickness) were prepared on BaF2 slides (Pier-Optics, Tatebayashi, Japan). FT-IR spectra were obtained using the Spectrum 100 Optica (PerkinElmer, Waltham, MA, USA) and Spotlight 400 (PerkinElmer, Waltham, MA, USA). The microscope was equipped with a computer-controlled x/y stage that permitted spectral sampling of the tissue in defined steps within a rectangular area. IR spectra were collected with an aperture diameter of 50 μm, and transmission from 4000 to 700 cm–1 with a spectral resolution of 4 cm–1 using an MCT detector. One hundred and twenty-eight scans per point were collected and averaged.
8
Collagen FTIR Spectroscopy and Microscopy
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ATR-FTIR spectroscopy was carried out using a Spectrum 400 (PerkinElmer, Walthan, MA, USA). Constructs were washed with molecular biology-grade water (3 × 15 min), then lyophilized in a Benchtop K series freeze dryer (VirTis, Gardiner, NY, USA) for 16 h at −103.2 °C and 11 mTorr. Analysis was performed at a resolution of 16 cm−1 with a total of 64 scans. The Fourier transformation algorithm was introduced by Spectrum (software) v.6.3.1 (2007) (PerkinElmer, Walthan, MA, USA). Incident radiation detected bond energies within mid-range infrared (650–2500 cm−1) and spectra were normalized to organic amide I in the 1680 to 1700 cm−1 footprint region for inter-chain amide-carbonyl bonds present in type I collagen.
For FTIR microscopy, a Spotlight 400 (PerkinElmer, Walthan, MA, USA) was attached to the ATR-FTIR apparatus to permit topographic assessment. The field of view was set to 100 µm by 200 µm of the sample, with a point size of 1.56 × 1.56 µm interval of −8.0 cm−1, and a resolution of 16 cm−1 over 16 scans per sampled point. The interferometer speed was set to 1 cm/s.
For FTIR microscopy, a Spotlight 400 (PerkinElmer, Walthan, MA, USA) was attached to the ATR-FTIR apparatus to permit topographic assessment. The field of view was set to 100 µm by 200 µm of the sample, with a point size of 1.56 × 1.56 µm interval of −8.0 cm−1, and a resolution of 16 cm−1 over 16 scans per sampled point. The interferometer speed was set to 1 cm/s.
9
Electrochemical and Structural Analysis of Polymer Electrolytes
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Successfully prepared electrolytes were firstly tested using an LCR meter (HIOKI 3531 Z Hi-tester, Nagano, Japan) to study their impedance properties and measure the real (Zr) and imaginary (Zi) parts of impedance. The measurement took place at room temperature with a frequency range of 50 Hz to 5 MHz. The DC potential for the experiment was 0.04 V. In this measurement, the polymer electrolyte samples with 2 cm in diameter (measure with a Vernier) were kept between two stainless-steel blocking electrodes under spring pressure. Field emission scanning electron microscopy (FESEM) was employed using a Hitachi SU8220 (Tokyo, Japan) at 500× magnification. The morphology of the samples was studied using the FESEM technique. On the other hand, the study on the interaction of the different components of the electrolytes, including polymers, salt, and plasticizer, was conducted using Fourier transform infrared (FTIR) spectroscopy. A Spotlight 400 Perkin–Elmer spectrometer was employed for this analysis with a resolution of 1 cm−1 (450–4000 cm−1). A deconvolution technique was used to extract any overlapping peaks. Correction of baseline and curve fitting were performed based on a Gaussian-Lorentzian function.
10
FTIR Spectroscopy of HPV Subtypes
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The samples (stored at −20 °C) were thawed (10 No-HPV, 7 LR-HPV, and 7 HR-HPV) and processed. The processing was characterized by the initial dilution in 0.5 mL of saline and homogenization by centrifugation at 4000 rpm for 2 min. Subsequently, 1 mL of SLH buffer (red cell lysis solution) was added to the fluid, which was centrifuged at 5000 rpm for 15 min. After this procedure, an additional centrifugation was performed at 5000 rpm for 15 min and the supernatant was discarded. This procedure was repeated three times for each sample. The formed pellet was used to carry out spectral measurements in the FTIR.
After processing each sample, 2 μl was applied to the Calcium Fluoride (CaF2) slide, four spectra per sample with 32 scans in the range of 750–4000 cm-1 at 4 cm-1 resolution were obtained FTIR spectrometer (Spotlight 400, PerkinElmer, USA) equipped with a microscope (Spotlight PerkinElmer 400, USA). All spectra were preprocessed by first derivatization, spectral range selection (1400-1800 cm-1 or 2800-3400 cm-1) and area normalization; and subjected to multivariate analysis Principal Component Analysis (PCA), PCA-Linear Discriminant Analysis (PC-LDA) and Leave One Out Cross Validation (LOOCV) in MATLAB 2015.
After processing each sample, 2 μl was applied to the Calcium Fluoride (CaF2) slide, four spectra per sample with 32 scans in the range of 750–4000 cm-1 at 4 cm-1 resolution were obtained FTIR spectrometer (Spotlight 400, PerkinElmer, USA) equipped with a microscope (Spotlight PerkinElmer 400, USA). All spectra were preprocessed by first derivatization, spectral range selection (1400-1800 cm-1 or 2800-3400 cm-1) and area normalization; and subjected to multivariate analysis Principal Component Analysis (PCA), PCA-Linear Discriminant Analysis (PC-LDA) and Leave One Out Cross Validation (LOOCV) in MATLAB 2015.
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