1D 1H NMR spectra were recorded on a Bruker AVANCE III HD spectrometer equipped with a 11.75 T magnet (1H Larmor frequency of 500 MHz) and a 5 mm BBO Prodigy CryoProbe (Bruker BioSpin) abbreviated as “500 MHz spectrometer” or a Bruker AVANCE III HD spectrometer equipped with a 7.0 T magnet (300 MHz) and a 5 mm BBFO probe abbreviated as “300 MHz spectrometer”. The frequency lock was set for 10% D2O and 90% H2O and, followed by phase and shim adjustments. The data was acquired using a perfect echo W5 WATERGATE solvent suppression pulse sequence (adapted PEW5) with the transmitter frequency offset (o1p) centered at water signal (4.7 ppm)23 (link)–25 (link). For product identification, 512 scans were accumulated with a relaxation delay (d1) of 5 s, size of FID (td) of 32k datapoints, and an acquisition time (aq) of 3.3 s. In addition, a presaturation sequence (zgpr) was employed for comparative studies. Data was acquired with Bruker TopSpin and processed (apodization with lb value of 0.2 Hz, zero filling, phasing) with Mnova software suite.
Bbfo probe
Manufactured by Bruker
Sourced in Germany, United States
The BBFO probe is a high-performance nuclear magnetic resonance (NMR) probe designed for use with Bruker's NMR spectrometers. It is capable of detecting a wide range of nuclei, including 1H, 13C, 15N, and 31P, making it a versatile tool for various analytical applications.
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Lab products found in correlation
Avance spectrometer, by Bruker (2 mentions)
Prodigy bbo cryoprobe, by Bruker (1 mentions)
Avance 3 hd, by Bruker (1 mentions)
Topspin v2, by Bruker (1 mentions)
Avance 3 600 mhz spectrometer, by Bruker (1 mentions)
Topspin 3.5pl7, by Bruker (1 mentions)
Samplejet autosampler, by Bruker (1 mentions)
Ascend 400 mhz spectrometer, by Bruker (1 mentions)
Pulse library, by Bruker (1 mentions)
Topspin 2, by Bruker (1 mentions)
Avance neo 600 mhz nmr spectrometer, by Bruker (1 mentions)
Onenmr probe, by Bruker (1 mentions)
Dd2 600 mhz nmr spectrometer, by Agilent Technologies (1 mentions)
Avance 3, by Bruker (1 mentions)
Avance 3 400 mhz, by Bruker (1 mentions)
Avance 3 hd 600 mhz wb spectrometer, by Bruker (1 mentions)
Drx spectrometer, by Bruker (1 mentions)
Avance 400 spectrometer, by Bruker (1 mentions)
Aviii 400 mhz spectrometer, by Bruker (1 mentions)
Fluoromax 4 spectrofluorometer, by Horiba (1 mentions)
16 protocols using bbfo probe
1
1D 1H NMR Analysis of Chemical Compounds
2
1H NMR Spectroscopy Protocol on Bruker Spectrometer
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The 1H NMR spectra was recorded on a Bruker Avance III HD spectrometer (Brucker Daltonic Inc., Bremen, Germany) using a 9.4 T magnet, corresponding to 1H resonance frequency of 400 MHz. A Bruker BBFO probe equipped with z gradients was used to accomplish automatic tuning and matching. Spectra were recorded with the following settings: pulse program (zg30) 30 pulse, TD = 64 K, 16 scans, the acquisition time of 3.98 s, relaxation delay of 1.0 s, and a sample temperature of 298.15 K. Spectra were processed using Bruker Topspin v2.1 (Bruker BioSpin AG). Free induction decay was multiplied by an exponential window with LB = 0.3 Hz.
3
NMR Metabolomics Profiling of Fecal Samples
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NMR data were recorded using Bruker 600MHz AVANCE III Spectrometer equipped with a BBFO + probe and a Sample Jet autosampler, which enabled the storage of 5 racks of 96 NMR tubes at 5 °C.
The sample temperature was controlled at 300 K during experiments. Spectra were recorded using the 1D Nuclear Over Hauser Effect spectroscopy pulse sequence (trd-90°-t1-90°-tm-90°-taq) with a relaxation delay (trd) of 24 s, a mixing time (tm) of 4 ms, and a t1 of 4 μs. The sequence enables optimal suppression of the water signal that dominates the spectrum. We collected 128 free induction decays (FIDs) of 65,532 data points using a spectral width of 12,019.230 kHz and an acquisition time of 2.726 s. The spectra were automatically phased and baseline corrected and referenced to the internal standard (TSP; δ = 0.0 ppm).
The relaxation delay was set at 24 s in order to reach the complete relaxation of all the metabolites between scans; this is a mandatory step in NMR when absolute concentration of the metabolites is calculated.
Two-dimensional (2D) NMR spectra were obtained to aid the assignment of fecal metabolites. The set of 2D experiments included 1H-1H correlation spectroscopy (COSY); 1H-1H total correlation spectroscopy (TOCSY), and 1H-13C heteronuclear single quantum correlation (HSQC) using the standard parameters implemented in Topspin 3.5pl7 (Bruker Biospin GmbH, Karlsruhe, Germany).
The sample temperature was controlled at 300 K during experiments. Spectra were recorded using the 1D Nuclear Over Hauser Effect spectroscopy pulse sequence (trd-90°-t1-90°-tm-90°-taq) with a relaxation delay (trd) of 24 s, a mixing time (tm) of 4 ms, and a t1 of 4 μs. The sequence enables optimal suppression of the water signal that dominates the spectrum. We collected 128 free induction decays (FIDs) of 65,532 data points using a spectral width of 12,019.230 kHz and an acquisition time of 2.726 s. The spectra were automatically phased and baseline corrected and referenced to the internal standard (TSP; δ = 0.0 ppm).
The relaxation delay was set at 24 s in order to reach the complete relaxation of all the metabolites between scans; this is a mandatory step in NMR when absolute concentration of the metabolites is calculated.
Two-dimensional (2D) NMR spectra were obtained to aid the assignment of fecal metabolites. The set of 2D experiments included 1H-1H correlation spectroscopy (COSY); 1H-1H total correlation spectroscopy (TOCSY), and 1H-13C heteronuclear single quantum correlation (HSQC) using the standard parameters implemented in Topspin 3.5pl7 (Bruker Biospin GmbH, Karlsruhe, Germany).
4
NMR Characterization of βCPCD Polymer
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When the βCPCD polymer was used, 1H NMR measurements were performed on a Bruker Ascend 400 MHz spectrometer with a BBFO probe to examine the solid phase after the washing process. When curcumin was mixed with the polymer in deuterated water (D2O) as previously described in Section 2.4 , a well-dispersed suspension was observed. The suspension was filtered using cotton wool and the solid was dried under high vacuum and re-dissolved in deuterated dimethyl sulfoxide (DMSO-d6) and the spectrum was recorded at ambient temperature for 16 scans. Signals representing the solvents served as internal standards. The solvent peaks were referenced at 2.5 ppm (DMSO-d6) and 4.7 ppm (HDO, H2O). Peak multiplicities were described as follows: singlet (s), multiplet (m) and broad (br).
5
NMR Spectroscopy of Bioactive Fractions
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The NMR sample was prepared by dissolving the bioactive fractions in 600 μl of deuterated water (D2O,). Then, 550 μl of the solution was transferred to 5-mm NMR tubes. NMR spectra were acquired using a Bruker 600 AVANAC III spectrometer equipped with a multinuclear broadband observe (BBFO) probe (BrukerBioSpin, Rheinstetten, Germany). To achieve a high signal-to-noise ratio, we recorded the 1H NMR spectra by collecting 4 k scans with a recycle delay time of 2 s. To suppress the water peak, we induced each spectrum with an excitation sculpting pulse sequence using a standard (zgesgp) program from the Bruker pulse library. The free induction decay (FID) data were collected with a spectral width of 18,028 Hz digitized into 32 k data points, and the FID signals were zero-filled and amplified by an exponential line-broadening factor of 1 Hz before Fourier transformation. Bruker’s Topspin 2.1 software was used in all experiments to collect and analyze the data.
6
NMR Spectroscopy of Thylakoid Membranes
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31P-NMR measurements were performed as described earlier29 (link). In detail, spectra were recorded on DD2 600 MHz NMR spectrometer (Agilent) using a OneNMR probe and Avance Neo 600 MHz NMR spectrometer (Bruker) using a BBFO probe, both tuned at the resonance frequency of the 31P nucleus, with 5 mm outer diameter tubes containing about 1.2 ml thylakoid suspension at a Chl content of about 8–10 mg/ml. As tested earlier, at this concentration, no magnetic orientation of the membranes occurs27 (link). The temperature was controlled within 0.1 °C; spectra were recorded using a 40°rf pulse, an interpulse time of 0.5 s and no 1H-decoupling. 31P chemical shifts are reported relative to 85% H3PO4 in water (δP = 0 ppm) used as an external reference. Spectral deconvolutions were performed by using the DMfit software70 (link).
7
Measuring 19F NMR Relaxation Times
8
Characterization of Organic Compounds
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The NMR spectra (1H, 13C, COSY, HSQC, HMBC) were recorded on a Bruker Avance III 400 MHz spectrometer (Bruker biospin, Billerica, USA), Bruker BBFO Probe. The coupling constant (J) is expressed in Hz.
9
Aqueous Mouse Liver Metabolomics NMR
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All 1H-NMR experiments were performed on a Bruker Avance III HD 600 MHz WB spectrometer (Karlsruhe, Germany) using a BBFO probe equipped with a z-axis field gradient at the NMR Core Facility at Academia Sinica (Taipei, Taiwan). The probe temperature was calibrated to 25 °C using methanol [26 (link)]. The 1H-NMR spectra of aqueous mouse liver extracts were acquired using a 90° pulse-and-acquire sequence. The acquisition parameters used included: number of scans = 32; number of dummy scans = 8; receiver gain = 1; spectral width = 10 kHz; acquisition time = 2 s; relaxation/recovery delay = 20 s; FID data points = 39,998; and 90° RF pulse duration = 18.9 µs. The FIDs were apodised using an exponential window function prior to Fourier transformation.
10
NMR Analysis of 13C Incorporation
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All NMR spectra were recorded in D2O on a Bruker Ultra Shield Plus AV-600 spectrometer (1H at 600 MHz, 13C at 151 MHz) with a 5 mm Bruker BBFO probe with methanol (100 μl) as an internal reference for all spectra at 49.5 p.p.m. Acquisition parameters were the same for all samples. Four spectra, each of 27,000 scans, were acquired for each sample pool. This was considered to give sufficient signal-to-noise ratio to identify incorporation of 13C into major metabolites of interest. NMR spectra were analysed using the Bruker Topspin v2.0 software interface. Detailed acquisition parameters can be found in Supplementary Table 1 .
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