The detection of liver sample metabolites for 1H-NMR analysis was performed on an Ascend 700 MHz spectrometer (Bruker, Billerica, MA, USA) coupled to an AVANCE NEO console equipped with a 5-millimeter triple resonance probe (Bruker, USA) at 298 K. For each sample, a one-dimensional 1H-NMR spectrum was acquired with water peak suppression using a nuclear Overhauser enhancement spectroscopy (NOESY) presaturation pulse sequence; 128 scans; 65,000 data points; an acquisition time of 2.4 s; a relaxation delay of 4 s; a mixing time of 10 milliseconds; and a spectral width of 20 ppm.
Avance neo console
Manufactured by Bruker
Sourced in United States
The AVANCE NEO console is a modular and flexible NMR spectrometer platform designed for high-performance nuclear magnetic resonance experiments. It provides advanced capabilities for a wide range of analytical applications.
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7 protocols using avance neo console
1
1H-NMR Analysis of Liver Metabolites
2
NMR Spectroscopy of Lactate Isotopomers
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All NMR spectra were recorded on a 600.23 MHz NMR, equipped with a 1.7 mm TCI CryoProbe and Avance Neo Console (Bruker Biospin). All NMR experiments were set up in the lock off followed by sweep off mode. 2H-decoupling off and on 1H-NMR spectra were acquired with a sequence that alternated decoupling with each scan. Relaxation delay (d1) of 1.5 s and acquisition time (AQ) of 2 s (3.5 s of recycling time, Tr) and a 90° pulse of 10.50 µs was used for acquisition of each of the spectra. The WET method containing selective pulses was applied on the strong water resonance55 (link). Waltz16 2H-decoupling sequence consists of a 90° pulse of 250 µs with decoupling power of 1.72 watts, producing a B1 of 1 kHz during the acquisition period. 13,157 complex data points were acquired with the spectral width of 11ppm. 128 scans were used to acquire each spectrum. 4 dummy scans were also used for equilibration of the spin states prior to acquisition. Modified T1 inversion recovery pulse sequence with 2H-decoupling on during the acquisition was used to measure the T1 of the lactate isotopomers and pyrazine standard. A relaxation delay (d1) of 50 s and inversion recovery delays (τ) of 0.001, 0.6, 0.9, 1.5, 2.0, 3.0, 6.0, 9.0, 14.0, 20.0, 30.0 and 40.0 s were used to determine the T1 of lactate isotopomers.
3
Solid-state NMR of Tin Compounds
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Solid-state
NMR experiments were performed at two different fields (B0 = 9.4 and 11.4 T). 119Sn was referenced indirectly
to 1H in a mixture of tetramethylsilane in CDCl3 and adamantane using IUPAC recommend frequencies.82 (link) NMR experiments at 9.4 T (400 MHz) were performed with
a wide-bore magnet equipped with a Bruker AVANCE III HD console. NMR
spectra were recorded on a 4.0 mm HXY MAS probe at a 12.5 kHz MAS. 119Sn pulse length for π/2 and π pulses were 1.75
and 3.5 μs, respectively, corresponding to a 143 kHz RF field.
Faster MAS frequencies was needed for experiments on Sn2SI2, thus a 2.5 mm HXY MAS probe was used. The 119Sn pulse length for π/2 and π pulses were 1.92 and 3.84
μs respectively, corresponding to an ca. 130 kHz Rf field. Experiments
at 14.1 T (600 MHz) were performed with a Bruker wide-bore magnet
equipped with a Bruker AVANCE NEO console. Experiments were recorded
on a 4.0 mm HXY MAS probe with 10 kHz MAS. π/2 and π pulse
lengths were 3.02 and 6.04 μs, corresponding to an ca. 83 kHz
Rf field. The 119Sn NMR spectrum of Sn2SI2 was measured on a 2.5 mm HXY MAS probe with a pulse length
of 1.96 and 3.92 μs for π/2 and π pulses. The 119Sn Rf field was ca. 128 kHz. All experiments were performed
with the probes configured in the double resonance (HX) mode to maximize
sensitivity.
NMR experiments were performed at two different fields (B0 = 9.4 and 11.4 T). 119Sn was referenced indirectly
to 1H in a mixture of tetramethylsilane in CDCl3 and adamantane using IUPAC recommend frequencies.82 (link) NMR experiments at 9.4 T (400 MHz) were performed with
a wide-bore magnet equipped with a Bruker AVANCE III HD console. NMR
spectra were recorded on a 4.0 mm HXY MAS probe at a 12.5 kHz MAS. 119Sn pulse length for π/2 and π pulses were 1.75
and 3.5 μs, respectively, corresponding to a 143 kHz RF field.
Faster MAS frequencies was needed for experiments on Sn2SI2, thus a 2.5 mm HXY MAS probe was used. The 119Sn pulse length for π/2 and π pulses were 1.92 and 3.84
μs respectively, corresponding to an ca. 130 kHz Rf field. Experiments
at 14.1 T (600 MHz) were performed with a Bruker wide-bore magnet
equipped with a Bruker AVANCE NEO console. Experiments were recorded
on a 4.0 mm HXY MAS probe with 10 kHz MAS. π/2 and π pulse
lengths were 3.02 and 6.04 μs, corresponding to an ca. 83 kHz
Rf field. The 119Sn NMR spectrum of Sn2SI2 was measured on a 2.5 mm HXY MAS probe with a pulse length
of 1.96 and 3.92 μs for π/2 and π pulses. The 119Sn Rf field was ca. 128 kHz. All experiments were performed
with the probes configured in the double resonance (HX) mode to maximize
sensitivity.
4
Quantitative NMR Analysis of Lipid Droplets
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1H and 2H NMR spectra of LDs were acquired on a 14.1 Tesla Bruker NMR system equipped with 1.7 mm TCI CryoProbe and Avance Neo console (Bruker BioSpin). The operating frequencies to acquire 1H and 2H NMR spectra were 600 and 92.14 MHz, respectively. For 1H NMR acquisition, a relaxation delay (d1) of 2 s, acquisition time of 2 s and 13,157 data points were digitized over a spectral width (sw) of 11 ppm. The deuterium lock channel was used to record 2H NMR data. Acquisition time of 2 s, relaxation delay of 2 s, flip angle of 90°, 2048 number of scans, acquired size (TD) of 2173 and spectral width of 11 ppm were used during the acquisition. All NMR spectra were acquired at 25°C. MestReNova (v14.0.1-23284, S.L, USA) software was used to process all of the NMR data. 1H NMR were Fourier transformed with an exponential line-broadening factor of 0.5 Hz and zero filling to 64 k data points followed by manual phase and automatic spline baseline correction. 2H NMR spectra were processed with 1.00 Hz exponential line broadening, zero filled to 8 k data points, manually phased and automatic splines baseline correction was applied. The peak fitting tool was used to extract the peak areas of fatty acid signals in 1H and 2H NMR spectra.
5
Quantitative NMR Analysis of Lipid Droplets
6
NMR Characterization of CH2O@C60
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Detailed NMR experiments were performed at 16.45 T, carried out using a Bruker Ascend 700 NB magnet fitted with a Bruker AVANCE NEO console and Bruker TCI prodigy 5 mm liquids cryoprobe. An approx. 23 mM solution of CH2O@C60 in 1,2-dichlorobenzene-d4 (ODCB-d4) was prepared by dissolving 14 mg of powdered CH2O@C60 (86.7% filling) in 0.8 mL of the solvent. The solution was then filtered and then degassed by bubbling nitrogen gas through the solution for 10 min. 1H and 13C NMR spectra were referenced to the solvent chemical shifts (1,2-dichlorobenzene-d4), 1H = 6.93 ppm and 13C = 127.19 ppm7 (link). All chemical shifts have confidence limits of ±0.01 ppm. NMR measurements on 13C-labelled 13CH2O@C60 were performed at 16.45 T on a 1 mM solution in toluene-d8, degassed by bubbling with nitrogen gas for 10 min.
7
Deuterium-labeled Metabolite Analysis by 2H-NMR
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A Bruker 14.1 T magnet system equipped with an Avance Neo Console (Bruker Biospin) and 1.7 mm CryoProbe was used to acquire 2H-NMR data of the deuterium-labeled metabolites in the cell media samples. The deuterium lock channel was used to acquire the 2H-NMR spectra at 92.12 MHz resonant frequency. An acquisition time (AQ) of 1 s and a relaxation delay (d1) of 2 s (total, 3 s of repetition time) with a 90° pulse was used to acquire all 2H-NMR spectra. A total of 4096 complex data points were digitized with the spectral width of 11 ppm using 256 scans for each of the 12 FIDs (3072 scans) for each of the samples. All NMR data were collected at room temperature (25 °C).
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