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Aviii spectrometer

Manufactured by Bruker
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Sourced in United States, Germany

The AVIII spectrometer is a high-performance nuclear magnetic resonance (NMR) instrument designed for advanced analytical applications. It provides precise and reliable measurements of molecular structures and dynamics.

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Lab products found in correlation

Sephadex lh 20, by Merck Group (6 mentions) Nicolet 380 ft ir instrument, by Thermo Fisher Scientific (4 mentions) Silica gel, by Qingdao Marine Chemical (4 mentions) Silica gel g plates, by Qingdao Marine Chemical (4 mentions) Mos 500 spectrometer, by Bio-Logic (2 mentions) Uv 2550 spectrometer, by Beckman Coulter (2 mentions) Api qstar pulsar mass spectrometer, by Bruker (2 mentions) Aviii 500 mhz spectrometer, by Bruker (2 mentions) Beckman du 640 spectrophotometer, by Beckman Coulter (1 mentions) Compact qqtof, by Bruker (1 mentions) Cosmosil pack, by Nacalai Tesque (1 mentions) Amazon sl, by Bruker (1 mentions) C18 column, by Agilent Technologies (1 mentions) Aviii 400 mhz, by Bruker (1 mentions) Microtof q, by Bruker (1 mentions) Ftir 8400s spectrometer, by Shimadzu (1 mentions) Aviii, by Bruker (1 mentions) 1h 13c 15n tci cryoprobe, by Bruker (1 mentions) Cobas 8000, by Roche (1 mentions) Combiflash rf, by Teledyne (1 mentions)

31 protocols using aviii spectrometer

1

Analytical Techniques for Natural Products

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Silica gel (60–80, 200–300 mesh, Qingdao Marine Chemical Co. Ltd.), ODS gel (20–45 m, Fuji Silysia Chemical Co. Ltd.), and Sephadex LH-20 (Merck, Kenilworth, NJ, United States) were used for column chromatography. Optical rotations were measured on a MCP 5100 modular compact polarimeter (Anton Paar, Austria). ECD spectra were recorded on a Bio-Logic Science MOS-500 spectrometer (Biologic, France). UV spectra were measured on a Beckman DU-640 spectrophotometer (Beckman Coulter, Inc., Brea, CA). IR absorptions were obtained on a Nicolet 380 FT-IR instrument (Thermo, Waltham, MA, United States) using KBr pellets. 1D and 2D NMR spectra were recorded on a Bruker AV III spectrometer (Bruker, United States; 1H NMR at 500 MHz and 13C NMR at 125 MHz for 1–3 and 5; 1H NMR at 600 MHz and 13C NMR at 150 MHz for 4, 6–8; and HMBC spectrum for 3) using TMS as the internal standard. ESIMS and HRESIMS were recorded with amaZon SL (Bruker, United States) or Compact QqTOF (Bruker, United States). Semipreparative HPLC was carried out using an ODS column and 5PFP column (Cosmosil-pack, 10 × 250 mm, 5 μm, 4 ml/min, Nacalai Tesque).
Cao X., Guo L., Cai C., Kong F., Yuan J., Gai C., Dai H., Wang P, & Mei W. (2021). Metabolites From the Mangrove-Derived Fungus Cladosporium sp. HNWSW-1. Frontiers in Chemistry, 9, 773703.
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2

Characterization of Organic Compounds

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1H NMR were recorded at 400 (Bruker AVIIIHD 400 MHz NMR with a broadband X-channel detect gradient probe) or 500 MHz (Avance AVIII 500 MHz spectrometer with a dual carbon/proton cryoprobe), and 13C were recorded at 125 MHz (Bruker AVIII spectrometer equipped with a cryogenically cooled carbon observe probe); chemical shifts are reported in δ (ppm) relative to the internal standard (CDCl3, 7.26 ppm or MeOD, 3.31 ppm). HRMS spectra were recorded with a LCT Premier (Waters Cor., Milford, MA). The purity of compounds was determined by HPLC (Agilent 1100 series quaternary pump; 60% MeCN/40% water; Agilent C-18 column, 4.6 mm × 150 mm, 5 μM) with UV detection. All biologically tested compounds were determined to be >95% pure. TLC analysis was performed on glass backed silica gel plates and visualized by UV light. All solvents were reagent grade and used without further purification.
Crowley V.M., Khandelwal A., Mishra S., Stothert A.R., Huard D.J., Zhao J., Muth A., Duerfeldt A.S., Kizziah J.L., Lieberman R.L., Dickey C.A, & Blagg B.S. (2016). Development of Glucose Regulated Protein 94-Selective Inhibitors Based on the BnIm and Radamide Scaffold. Journal of medicinal chemistry, 59(7), 3471-3488.
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3

Solid-State 13C NMR Spectroscopy of Cellulose

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The solid-state CP/MAS 13C NMR spectra were recorded on a Bruker AVIII-400 MHz with a 4 mm HR MAS BL4 probe. The spectroscopy of cellulose samples for solid state CP-MAS (cross-polarisation, magic anglespinning) 13C NMR spectroscopy was obtained on a Bruker AVIII spectrometer (Bruker, Germany) and the span rate of the 4 mm rotor was 12 kHZ for the test. The acquisition time was 0.0127 s, and the recycle delay was 2.0 s.
Xin P.P., Huang Y.B., Hse C.Y., Cheng H.N., Huang C, & Pan H. (2017). Modification of Cellulose with Succinic Anhydride in TBAA/DMSO Mixed Solvent under Catalyst-Free Conditions. Materials, 10(5), 526.
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4

Characterization of Organic Compounds

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Reagents were obtained from commercial suppliers and used without further purification. Acetonitrile (ACN) was dried using a Puresolv solvent. The reaction under an inert atmosphere was carried out using oven-dried glassware and solvents were added via syringe. 1H, 13C and 31P NMR spectra were obtained on a Bruker AVIII spectrometer operating at 400, 101, and 162 MHz, respectively or a Bruker AVIII operating at 500, 126, and 162 MHz, respectively. All coupling constants were measured in Hertz. Deuterated solvents contained trimethylsilane (TMS) as a reference compound. DEPT was used to assign the signals in 13C NMR spectra as C, CH, CH2 and CH3. Mass spectra (MS) were recorded on a Jeol JMS700 (MStation) spectrometer for EI and CI or Bruker Microtof-q for ESI. A Shimadzu FTIR-8400S spectrometer was used to obtain infrared (IR) spectra. Purification by used a Biotage Isolera automated system.
Booty L.M., Gawel J.M., Cvetko F., Caldwell S.T., Hall A.R., Mulvey J.F., James A.M., Hinchy E.C., Prime T.A., Arndt S., Beninca C., Bright T.P., Clatworthy M.R., Ferdinand J.R., Prag H.A., Logan A., Prudent J., Krieg T., Hartley R.C, & Murphy M.P. (2019). Selective Disruption of Mitochondrial Thiol Redox State in Cells and In Vivo. Cell Chemical Biology, 26(3), 449-461.e8.
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5

NMR Spectroscopy of Chemical Compounds

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The NMR spectra were recorded on a Bruker AV-III spectrometer equipped with 5 mm probes at 298 K. Chemical shifts were provided on the δ scale and referenced to TMS at 0.00 ppm for proton and carbon. The coupling constants (J) are in hertz. The pulse conditions are presented in Supplementary Table S2.
Xue B.X., Yang T.T., He R.S., Gao W.K., Lai J.X., Liu S.X., Duan C.Y., Wang S.X., Yu H.J., Yang W.Z., Zhang L.H., Wang Q.L, & Wu H.H. (2023). Degradation Profiling of Nardosinone at High Temperature and in Simulated Gastric and Intestinal Fluids. Molecules, 28(14), 5382.
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6

Absolute Quantification of CSF Metabolites

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100 µL of CSF was diluted with 450 μL of 75 mM sodium phosphate buffer D2O (pH 7.4) containing 1 mM maleic acid as an internal reference standard. Samples were centrifuged at 3,000 x g for 5 minutes before transferring to a 5-mm NMR tube. NMR spectra were acquired at 310 K using a 700-MHz Bruker AVIII spectrometer operating at 16.4 T equipped with a 1H [13C/15N] TCI cryoprobe (Department of Chemistry, University of Oxford) and processed as previously described (16 (link)).
NMR metabolite measures were converted to absolute concentrations using the internal reference standard (1 mM maleic acid) as previously described (16 (link)). To validate the quantification of the metabolites by NMR, the glucose and lactate levels in all CSF samples were measured using a Cobas® 8000 modular analyser (Roche Diagnostics, Switzerland) coupled with the Gluc3 and LAC2 assays, respectively.
Probert F., Yeo T., Zhou Y., Sealey M., Arora S., Palace J., Claridge T.D., Hillenbrand R., Oechtering J., Kuhle J., Leppert D, & Anthony D.C. (2022). Determination of CSF GFAP, CCN5, and vWF Levels Enhances the Diagnostic Accuracy of Clinically Defined MS From Non-MS Patients With CSF Oligoclonal Bands. Frontiers in Immunology, 12, 811351.
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7

Global Metabolomics via NMR Spectroscopy

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Global metabolomics detects all measurable metabolites in a sample and is ideal for comprehensive biochemical profiling for biomarker discovery. All 1H NMR experiments for global metabolomics were performed at the Department of Chemistry, University of Oxford, using a 700-MHz Bruker AVIII spectrometer, with the Carr–Purcell–Meiboom–Gill (CPMG) relaxation editing pulse sequence for spectra acquisition. Technical details of NMR sample preparation, experiments and spectra processing have been previously published.13 (link),16 (link) Integral values of individual spectral ‘bins’ were computed with constant-sum-normalization and used as quantitative variables expressed in arbitrary units (AU). In all, 191 metabolite ‘bins’ were available for multivariate statistical analysis. Metabolite assignments were performed by referencing to literature values and the Human Metabolome Database,21 (link) as well as inspection of the 1D total correlation spectroscopy spectra.
Yeo T., Probert F., Sealey M., Saldana L., Geraldes R., Höckner S., Schiffer E., Claridge T.D., Leppert D., DeLuca G., Kuhle J., Palace J, & Anthony D.C. (2021). Objective biomarkers for clinical relapse in multiple sclerosis: a metabolomics approach. Brain Communications, 3(4), fcab240.
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8

Chiral Analysis of Small Molecules

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All chemical reagents were purchased from commercial suppliers and used without further purification. Flash column chromatography was performed on silica gel (4—63 mm) from Sorbent Technologies. Separation was also performed with a Teledyne Isco CombiFlash Rf. Microwaved reactions took place in a Biotage Microwave reactor. 1H and 13C nuclear magnetic resonance (NMR) spectra were recorded using a 500 MHz Bruker AVIII spectrometer equipped with a cryogenically cooled carbon observe probe using tetramethylsilane as an internal standard. Chemical shifts (δ) are reported in parts per million, and coupling constants (J) are reported in hertz. The high-resolution mass spectrum (HRMS) was recorded on an LCT Premier (Micromass Ltd., Manchester, U.K.) time-of-flight mass spectrometer with an electrospray ion source in either positive or negative mode. Melting points were measured with a Thomas capillary melting point apparatus and are uncorrected. Chiral analysis was conducted on an Agilent 1200 RRLC instrument with a photodiode array on a Chiralpak ID column.
Meneely K.M., Ronnebaum T.A., Riley A.P., Prisinzano T.E, & Lamb A.L. (2016). Holo Structure and Steady State Kinetics of the Thiazolinyl Imine Reductases for Siderophore Biosynthesis. Biochemistry, 55(38), 5423-5433.
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9

Comprehensive Spectroscopic Characterization

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The 1H, 13C, and 2D NMR spectra were recorded on a Bruker AV III spectrometer (Bruker, Bremen, Germany) at either 500 MHz (1H) or 125 MHz (13C) using TMS as an internal standard. The HRMS were measured with an API QSTAR Pulsar mass spectrometer (Bruker). The UV spectra were performed on a Shimadzu UV-2550 spectrometer (Beckman, Brea, CA, USA). The IR absorptions were obtained on a Nicolet 380 FT-IR instrument (Thermo, Pittsburgh, PA, USA) using KBr pellets. The optical rotation was measured on a Rudolph Autopol III polarimeter (Rudolph, Hackettstown, NJ, USA). Silica gel (60–80, 200–300 mesh, Qingdao Marine Chemical Co. Ltd., Qingdao, China), ODS gel (20–45 μm, Fuji Silysia Chemical Co. Ltd., Durham, NC, USA), and Sephadex LH-20 (Merck, Darmstadt, Germany) were used for column chromatography. The TLC was conducted on pre-coated silica gel G plates (Qingdao Marine Chemical Co. Ltd.), and spots were detected by spraying with 10% H2SO4 in EtOH followed by heating.
Mi C.N., Wang H., Chen H.Q., Cai C.H., Li S.P., Mei W.L, & Dai H.F. (2019). Polyacetylenes from the Roots of Swietenia macrophylla King. Molecules, 24(7), 1291.
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10

Bicelle-Mediated Cavitand-Guest Exchange

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Bicelle samples containing guest 7 and cavitand were loaded in a 4 mm Bruker solid-state rotor, and experiments were performed on a Bruker AVIII spectrometer equipped with a 1H-X double resonance 4 mm MAS probe with no spinning. The 2D EXSY spectra of the cavitand:guest 7 exchange process in bicelles were recorded at 316 K at 9.4 T with a NOESY pulse sequence. Each of the 128 F1 increments was the accumulation of 128 scans with a relaxation delay of 3 s. Before Fourier transformation the FID was multiplied by a 90° sine square function in the F1 domain and an EM function in the F2 domain. 2 K (F2) _ 256 (F1) real data points were used with a resolution of 1 Hz per point.
Perez L., Caulkins B.G., Mettry M., Mueller L.J, & Hooley R.J. (2018). Lipid bilayer environments control exchange kinetics of deep cavitand hosts and enhance disfavored guest conformations †Electronic supplementary information (ESI) available: Spectral data not included in the text, detailed description of the exchange fitting process. See DOI: 10.1039/c7sc05155g. Chemical Science, 9(7), 1836-1845.
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