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Expression cms mass spectrometer

Manufactured by Advion
Sourced in United States

The Expression CMS mass spectrometer is a laboratory instrument designed for the detection and analysis of chemical compounds. It functions by ionizing and separating molecules based on their mass-to-charge ratio, providing users with detailed information about the composition and structure of the samples being analyzed.

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3 protocols using expression cms mass spectrometer

1

Synthesis and Characterization of Stereoisomeric Compounds

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Example 1

1. Materials and Methods

Experimental

All buffers and reagents were obtained from Fisher Scientific or Sigma-Aldrich and used without further purification. Synthetic reactions were monitored by TLC using precoated silica gel plates (Silicycle 60F254, 0.25 mm thickness). Compounds were detected by ultraviolet light (λ=254 nm) followed by visualization with ammonium molybdate (10% w/v in 2M H2SO4), permanganate (1% w/v in water), or ninhydrin (1.5% w/v solution in butanol), with heating. Flash chromatography was performed using Silicyle silica gel (230-400 mesh). NMR spectra were obtained using a Varian Unity Inova 500 MHz spectrometer dissolving samples in the appropriate deuterated solvents (CDCl3, or CD3OD). Chemical shifts were reported in ppm downfield from tetramethylsilane. Low resolution ESI mass spectrometry was performed on an Advion Expression CMS Mass Spectrometer.

The compounds in the synthetic procedures of Example 1 are present as a mixture of enantiomers having the following stereochemical configurations:

[Figure (not displayed)]

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2

Anhydrous Organic Synthesis Protocols

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All chemicals were obtained from Thermo Fisher Scientific (Seoul, Korea), SEJIN CI Co. (Seoul, Korea), or Sigma-Aldrich (St. Louis, MO, USA). Reagents purchased were used without further purification. Solvents requiring anhydrous conditions were distilled over CaH2, or Na and benzophenone before use. Reactions were carried out in a nitrogen atmosphere and analyzed by thin layer chromatography (TLC) using pre-coated 60F245 plates purchased from Merck. Flash column chromatography using MP Silica 40–63, 60 Å was performed. Subsequently, 1H, 13C, and 19F NMR were measured at 500, 125, and 470 MHz, respectively. Mass data for low resolution were recorded in ESI modes (positive and negative) using an Expression CMS mass spectrometer (Advion Ithaca, NY, USA). CDCl3, CD3OD, and DMSO-d6 were used as solvents for NMR. All chemical shifts were measured in ppm (parts per million) versus residual solvent or deuterated peaks (δH 7.26, δH 3.31, and δH 2.48 for CDCl3, CD3OD, and DMSO-d6, respectively, and δC 77.0, δC 49.0, and δC 40.0 for CDCl3, CD3OD, and DMSO-d6, respectively). Coupling constants (J) are represented in hertz (Hz). The following abbreviations for 1H NMR were used: dd (doublet of doublets), brs (broad singlet), s (singlet), q (quartet), t (triplet), and d (doublet).
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3

Optimization of Angiotensin Photoredox Reaction

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Initial optimization with angiotensin was studied using a Waters Acquity ultrahigh-performance liquid chromatography (UPLC) (Empower Software) connected to an Advion Expression CMS mass spectrometer. Method: Solvent A: acetonitrile, Solvent B: water, (5% A and 95% B, 0–2 min; 10% A and 90%, 2–3 min; 20% A and 80% B, 3–10 min; 30% A and 70% B, 10–12 min; 95% A and 5% B, 12–16.5 min; 95% A and 5% B, 16.5–18 min; 5% A and 95% B, 18–20 min). For the further optimization of angiotensin at UT-Austin, LC/MS were recorded on an Agilent Technologies 6120 Single Quadrupole or 6130 Single Quadrupole interfaced with an Agilent 1200 series LC system equipped with a diode-array detector. The resulting spectra were analyzed using Agilent LC/MSD ChemStation. All LC experiments were run with a 5–95% gradient elution (methanol/water) over 15 min. The conversion was calculated by the ratio of the peak areas of C-terminal-modified angiotensin and p-toluic acid (internal standard) under UV trace for angiotensin photoredox reaction optimization reaction (Supporting Information Table 1–4) For the determination of conversions of peptides with varying C-terminal AAs (Table 1), the value was obtained by dividing the peak area of the C-terminal modified product by the addition of peak areas of the C-terminal modified product and unreacted starting materials under the total ion chromatogram (TIC).
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