Synthetic procedures and data for final compounds which were evaluated for biological activity is provided. Full synthesis details including the production of intermediates (designated as IM-1, IM-2, etc.) and schemes are given in the Supporting Information . All chemicals used were of reagent grade. Product formation was monitored by 1H and 13C NMR spectroscopy on Varian or Bruker spectrometers at 400 or 500 MHz for 1H. Chemical shifts are reported in parts per million (ppm) from residual chloroform using the convention that low-field, high-frequency, paramagnetic or deshielded shifts are positive (IUPAC δ-scale). Purity was determined by 1H quantitative NMR (qNMR) at 500 MHz using a Bruker Avance III HD NMR Spectrometer equipped with a BBFO CryoProbe, using Mnova software, as well as by using high-resolution mass spectrometry (HRMS).
Bbfo cryoprobe
Manufactured by Bruker
Sourced in Germany
The BBFO CryoProbe is a high-performance nuclear magnetic resonance (NMR) probe designed for Bruker spectrometers. It is optimized for cryogenic operation, providing enhanced sensitivity and resolution for a wide range of NMR experiments.
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4 protocols using bbfo cryoprobe
1
Synthetic Procedures and Biological Data
2
NMR Spectroscopic Analysis of Chemical Compounds
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All NMR measurements were performed at 298 K on a Bruker Avance III 600 MHz NMR spectrometer equipped with a BBFO cryoprobe (Bruker Bio Spin, Rheinstetten, Germany). One-dimensional (1D) 1H spectra were acquired using the pulse sequence NOESYGPPR1D [RD-G1- 90°-t-90°-τm-G2-90°-ACQ] with the following acquisition parameters: relaxation delay (RD), 4 s; short delay (t), 4 μs; mixing time (τm), 10 ms; spectral width, 20 ppm; acquisition time, 1.93 s; and 128 transients. The methyl groups of the TSP molecule were set at 0 ppm for chemical shift calibration. The two-dimensional (2D) 1H–13C heteronuclear single quantum coherence (HSQC) spectrum was recorded with a spectral width of 10 ppm in the 1H dimension and 110 ppm in the 13C dimension, a data matrix of 1024 × 256 points, and a relaxation delay of 1.5 s. The 2D total correlation spectroscopy (TOCSY) spectrum was recorded with a spectral width of 10 ppm in both 1H dimensions, a data matrix of 2048 × 256 points, and a relaxation delay of 1.5 s.
3
NMR Spectroscopy of Gastric Tissue Metabolites
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One‐dimensional (1D) 1H‐NMR experiments were carried out on a Bruker AVANCE III 600 MHz spectrometer (Bruker BioSpin) equipped with a BBFO CryoProbe at 298 K. The spectra of aqueous extracts of gastric tissues were recorded on BRUKER NMR Spectrometer by using the pulse sequence NOESYGPPR1D (RD‐90°‐t1‐90°‐τm‐90°‐ACQ) with water suppression during the relaxation delay (RD) and mixing time (τm).19 The RD was 4 s, t1 was a short delay (4 μs), and τm was 10 ms. A total of 32 transients were collected into 64K data points using a spectral width of 12 kHz with an acquisition time (ACQ) of 2.73 s.
Furthermore, 2D 1H‐1H total correlation spectroscopy (TOCSY) was acquired for selected NMR samples on a Bruker AVANCE III 850 MHz spectrometer with a TCI CryoProbe at 298K. The experimental parameters were detailed in previous reports.20 , 21 , 22 Resonance assignments of metabolites were carried out based on the 1D 1H‐spectra using a combination of Chenomx NMR Suite (version 7.1) and the Human Metabolome Data Base (https://hmdb.ca/ ), referring to relevant published references. The assigned metabolites were confirmed by 2D TOCSY spectrum.
Furthermore, 2D 1H‐1H total correlation spectroscopy (TOCSY) was acquired for selected NMR samples on a Bruker AVANCE III 850 MHz spectrometer with a TCI CryoProbe at 298K. The experimental parameters were detailed in previous reports.
4
NMR Spectroscopy of Amphipathic Peptides
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The peptides were dissolved directly in 50 mM Tris (pH 7.4) or in a d 3 -TFE/buffer (1 : 3 v/v) solution to give a nal peptide concentration of 1 mg mL À1 . Trimethylsilylpropanoic acid (TSP) was added as an internal chemical shi reference. Two-dimensional 1 H-1 H TOCSY, 1 H-1 H NOESY and 1 H-13 C HSQC spectra were acquired on a 500 MHz Bruker spectrometer equipped with a BBFO cryo probe (Bruker Biospin, Rheinstetten, Germany). Assignment was based on TOCSY and NOESY cross-peaks as well as typical amino acid chemical shis. The secondary structural propensity was calculated based on proton (H, HA, HB) and carbon (CA, CB) chemical shis for all residues. The neighbour corrected Structural Propensity Calculator (ncSPC) 62 online tool compensating for the neighbour effects was used for the calculation, in order to obtain the most accurate structural propensities: https://st-protein02.chem.au.dk/ncSPC/.
For the samples of PGLa and magainin 2a dissolved in aqueous buffer (50 mM Tris, pH 7.4), the assignments were based on the random coil chemical shis calculated by the same online tool. As no correlations were observed in the NOESY spectra and only small deviations from the random coil shis were observed, we consider the results to be reliable.
For the samples of PGLa and magainin 2a dissolved in aqueous buffer (50 mM Tris, pH 7.4), the assignments were based on the random coil chemical shis calculated by the same online tool. As no correlations were observed in the NOESY spectra and only small deviations from the random coil shis were observed, we consider the results to be reliable.
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