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Lct premier micromass spectrometer

Manufactured by Waters Corporation
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The LCT premier micromass spectrometer is a laboratory instrument designed for high-performance liquid chromatography mass spectrometry (LC-MS) analysis. It provides accurate mass measurement and enhanced sensitivity for a wide range of applications.

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Lab products found in correlation

Drx 500 mhz, by Bruker (2 mentions) Avance 600 mhz, by Bruker (2 mentions) Drx 400 mhz, by Bruker (2 mentions) Hplc system, by Gilson (1 mentions) Silica gel 60, by Thermo Fisher Scientific (1 mentions) Uplc beh c18, by Waters Corporation (1 mentions) Silica gel 60 f254 aluminum plates, by Merck Group (1 mentions)

Close spelling variants of this product

Micromass LCT Premier XE Mass Spectrometer LCT Premier XE Micromass Waters spectrometer Micromass LCT Premier Mass Spectrometer Micromass-LCT Premier Time of Flight (TOF) mass spectrometer LCT Premier XE Micromass spectrometer Micromass LCT Premier LCT Premier

4 protocols using lct premier micromass spectrometer

1

Preparative HPLC Purification of Peptides

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The peptides were purified on a preparative Gilson HPLC system (Gilson Inc., Middleton, WI, USA) using a reversed phase HPLC column (Phenomenex Inc., Torrance, CA, USA) as specified in the supporting experimental section. Two mobile phases were used for elution: A = 0.1% TFA in deionized water (Veolia, Saint-Maurice, France) and B = 0.1% TFA in acetonitrile using a linear gradient. Relevant fractions were selected by analytical LC-MS (Waters Acquity H-class HPLC coupled to LCT premier micromass spectrometer; Waters Corp., Milford, MA, USA) and fractions containing the pure peptide were pooled and lyophilized.
Huppelschoten Y., Buchardt J., Nielsen T.E., Sapmaz A, & van der Heden van Noort G.J. (2023). Total Chemical Synthesis of LC3A and LC3B Activity-Based Probes. Biomedicines, 11(3), 884.
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2

Synthesis and Purification of Peptide 11

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Peptide 4 (18.7 mg, 0.0020 mmol) and peptide 9 (12.1 mg, 0.0025 mmol) were dissolved in 6 M Gdn.HCl/0.2 M NaH2PO4, pH 7.2 at a final concentration of 1 mM. Mercaptophenylacetic acid (MPAA) and tris(2-carboxyethyl)phosphine (TCEP) were added from a 1 M stock in deionized water to a final concentration of 100 mM and 25 mM. Then, pH was adjusted to 7.0 and the reaction was shaken for 16 h at 37 °C upon which LC-MS analysis (Waters Acquity H-class HPLC coupled to a LCT premier micromass spectrometer; Waters Corp., Milford, MA, USA) showed that the reaction was complete. The crude peptide was purified by preparative HPLC using a Gemini® (Phenomenex Inc., Torrance, CA, USA) 110 Å, C4, 5 μm, 10 mm × 250 mm column (25 to 45% B over 20 min, 5 mL/min). Lyophilization afforded peptide 11 as a white solid (2.59 mg, 8.9% yield), calculated mass: 14,715.1 Da, observed: 14,716.0 Da.
Huppelschoten Y., Buchardt J., Nielsen T.E., Sapmaz A, & van der Heden van Noort G.J. (2023). Total Chemical Synthesis of LC3A and LC3B Activity-Based Probes. Biomedicines, 11(3), 884.
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3

Synthesis of Organic Compounds

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All reactions were performed with commercially available reagents (Aldrich, Thermo-Fisher, Alfa Aesar, Acros, Oakwood, Millipore) without further purification. Anhydrous solvents were acquired through a solvent purification system (Inert PureSolv and JC Meyer systems) or purified according to standard procedures. 1H NMR spectra were recorded on Bruker DRX 400 MHz, Bruker DRX 500 MHz, or Bruker Avance 600 MHz spectrometer and processed using TopSpin 3.5 software. LRMS and HRMS data were obtained via ESI LC-TOF on a Waters (Micromass) LCT Premier spectrometer (Waters), with PEG as the calibrant for HRMS. Optical rotation was recorded on a Rudolph Autopol III Automatic Polarimeter at room temperature in methanol. TLC was performed using EMD Millipore silica gel 60 F254 aluminum plates. Separation by column chromatography was conducted using Fisher silica gel 60 (230–400 mesh). Purity of final products was verified by 1H NMR with TMS as a standard and by UPLC-MS (Waters Acquity UPLC H-class QDA with a FTN) with a C18 column (2.1 x 50 mm; Acquity UPLC BEH C18; 1.7 μm particles). All investigated compounds were >95% pure as determined by UPLC-MS. High resolution mass spectrometry data, NMR spectra, and UPLC-MS chromatograms are included in the Supplementary Material.
Samuels E.R, & Sevrioukova I.F. (2020). An increase in side-group hydrophobicity largely improves the potency of ritonavir-like inhibitors of CYP3A4. Bioorganic & medicinal chemistry, 28(6), 115349.
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4

General Chemistry Analytical Methods

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General Chemistry Methods—1H NMR spectra were recorded on Bruker DRX 400 MHz, Bruker DRX 500 MHz, or Bruker Avance 600 MHz spectrometers. Chemical shifts (δ) were reported in ppm for the solution of the compound in CD3OD or CDCl3 (with internal reference TMS), and J values in hertz. NMR data were processed using TopSpin 3.5 software, and ACD/Spectrus Processor 2018.2.5. LRMS and HRMS data were obtained via ESI LC-TOF on a Waters (Micromass) LCT Premier spectrometer (Waters), with PEG as the calibrant for HRMS. The optical rotation was recorded on a Rudolph Autopol III Automatic Polarimeter at room temperature in MeOH. The purity of the final products was verified by NMR with TMS as a standard. TLC was performed using EMD Millipore silica gel 60 F254 aluminum plates. Separation by column chromatography was performed using Fisher silica gel 60 (230–400 mesh). All reactions were performed with commercially available reagents (Aldrich, Thermo-Fisher, Alfa Aesar, Acros, Oakwood, and Millipore). Anhydrous solvents were acquired using a solvent purification system (Inert PureSolv and JC Meyer systems) or purified according to standard procedures.
Samuels E.R, & Sevrioukova I.F. (2022). Interaction of CYP3A4 with Rationally Designed Ritonavir Analogues: Impact of Steric Constraints Imposed on the Heme-Ligating Group and the End-Pyridine Attachment. International Journal of Molecular Sciences, 23(13), 7291.
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