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4 protocols using ft ir nicolet is5 spectrometer

1

Cellulose Structural Changes via FTIR

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The structural changes in cellulose after enzymatic treatment was confirmed by the FTIR spectroscopy. The spectra were obtained using a pelleting technique—1 mg cellulose was mixed with 200 mg bromide potassium (KBr, Sigma-Aldrich, Steinchein, Germany). Spectra were registered using an FTIR Nicolet iS5 spectrometer (Thermo Fisher Scientific, Madison, WI, USA) at a range from 4000 to 500 cm−1 at a resolution of 4 cm−1, registering 16 scans.
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2

Spectroscopic Analysis and Amyloid Aggregation Inhibition

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IR spectra were measured using a Thermo Scientific FT-IR Nicolet iS5 spectrometer (ATR). UV spectra were measured using a Thermo Scientific UV–Vis GENESYS 10S spectrophotometer. ECD spectra were measured with a Jasco J-820 circular dichroism spectropolarimeter (JASCO, Tokyo, Japan). 1H- and 13C-NMR spectra were recorded using a JNM-AL 400 MHz and JNM-ECZ 400 MHz spectrometer (JEOL, Tokyo, Japan). HREIMS and HRFABMS spectra were obtained using a JEOL JMS-700 spectrometer (JEOL). Column chromatography was carried out with silica gel 60 N (63–210 μm, Kanto Chemical, Tokyo, Japan) and ODS silica gel YMC-GEL ODS-A (YMC, Kyoto, Japan). MPLC was performed using a Pure C-850 FlashPrep (BUCHI, Flawil, Switzerland) and a series of Flash Cartridges (BUCHI, Flawil, Switzerland). Semi-preparative HPLC was conducted using a Jasco PU-2080 Plus pump (JASCO) and a Jasco UV-2075 Plus UV/VIS detector at 220 or 254 nm (JASCO). Inhibition of Aβ aggregation was assayed using a Synergy HTX Multi-Mode Reader (BioTek, Winooski, VT, USA), Aβ40 peptide (Peptide Institute, Osaka, Japan), thioflavin-T (FUJIFILM Wako, Osaka, Japan), 25% ammonia solution (FUJIFILM Wako), and dimethyl sulfoxide (FUJIFILM Wako).
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3

Temperature-Dependent FT-IR Spectroscopy

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The FT-IR Nicolet iS5 spectrometer (Thermo Scientific, Madison, WI, USA) was used to collect FT-IR spectra with a wavenumber ranging from 4000 cm−1 to 400 cm−1. To record the spectra at different temperatures, the samples were analyzed using the same spectrometer equipped with an attenuated total reflection accessory (Pike Technologies, Madison, WI, USA) on a heatable germanium crystal (up to 120 °C) in transmission mode (64 scans and 4 cm−1 resolution). The chosen temperature range was 25–100 °C, with a heating and cooling rate of 10 °C/min.
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4

Characterization and Evaluation of Aβ Aggregation Inhibitors

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Optical rotation values were recorded with a Horiba SEPA-300 polarimeter. IR spectra were measured with a Thermo FT-IR Nicolet iS5 spectrometer (ATR). 1H- and 13C-NMR spectra were recorded using a JNM LA-500 spectrometer. HRFABMS spectra were obtained using a JEOL JMS-700 spectrometer. Column chromatography was carried out with silica gel 60 N (63–210 μm) from Kanto Chemical, ODS silica gel YMC-GEL ODS-A from YMC Co. Ltd., and Diaion HP-20 from Mitsubishi Chemical Co. Ion-exchange chromatography was performed using Dowex 50 W-X8 resin (50–100 mesh, H-form) from Sigma-Aldrich. Thin-layer chromatography was carried out using TLC silica gel 60F254 and RP-18 F254S plates from Merck. Inhibition of Aβ aggregation was assayed using a Synergy HTX Multi-Mode Reader (BioTek, Winooski, Vermont, USA), Aβ40 (Peptide Institute, Osaka, Japan), and thioflavin-T (Fujifilm-Wako).
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