Maldi ltq orbitrap xl

Manufactured by Thermo Fisher Scientific

Sourced in Germany, United States

The MALDI LTQ Orbitrap XL is a high-performance mass spectrometry system that combines the MALDI (Matrix-Assisted Laser Desorption/Ionization) ion source with the LTQ Orbitrap hybrid mass analyzer. It provides accurate mass measurement and high-resolution capabilities for a wide range of biomolecular applications.

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36 protocols using maldi ltq orbitrap xl

MALDI-MS Imaging of Tissue Sections

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Sections were inspected under light microscopy to determine quality (i.e., intact tissue, no cosmetic defects) and coated with 2,5-dihydroxybenzoic acid (DHB) by sublimation as described by Hankin et al. [49 (link)].
Matrix-coated sections were imaged using a MALDI-LTQ-Orbitrap-XL mass spectrometer (ThermoFisher Scientific, San Jose, CA, USA). All sections to image PC were collected in positive ionization mode. The MALDI ionization parameters were set as: 12 μJ/pulse, 10 laser shots per step, and 40 μm step size. The Orbitrap mass analyzer was set to collect from m/z 600 to 1200 with a set resolution of 100,000. LTQ Tune Plus and Xcalibur software (Thermo Scientific) were used to operate the instrument and collect the raw data.

Romsdahl T.B., Kambhampati S., Koley S., Yadav U.P., Alonso A.P., Allen D.K, & Chapman K.D. (2021). Analyzing Mass Spectrometry Imaging Data of 13C-Labeled Phospholipids in Camelina sativa and Thlaspi arvense (Pennycress) Embryos. Metabolites, 11(3), 148.

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MALDI-TOF Analysis of Compounds

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Drugs were dissolved in 50% methanol (Sigma-Aldrich, Steinheim, Germany) at HPLC grade (99.8+%) at 0.5 mg/mL concentration. The matrix (7.5 mg/mL α-cyano-4-hydroxycinnamic acid, Sigma Aldrich, Steinheim, Germany) was dissolved in 50% acetonitrile at hypergrade for liquid chromatography-mass spectrometry (LC-MS, Merck, Darmstadt, Germany) and 0.1% trifluoroacetic acid (Sigma-Aldrich, Steinheim, Germany). 1μL of the compound solution was applied with 1μL matrix solution to the MALDI plate. Full mass spectra were obtained by using a MALDI LTQ Orbitrap XL mass spectrometer (Thermo Fisher Scientific, Bremen, Germany) at 60,000 resolution in positive polarity mode. The spots were sampled in survey mode collecting 20 experiments for a single run. The nitrogen laser was set to 10 μJ. The detected precursor ion was fragmentized by using 40% normalized collision energy (NCE) during a 30 ms activation time, while activation Q of 0.250 was applied. The precursor ions were isolated with m/z 2.0 width and MS/MS spectra were collected at normal scan rate in centroid mode.

Torok S., Rezeli M., Kelemen O., Vegvari A., Watanabe K., Sugihara Y., Tisza A., Marton T., Kovacs I., Tovari J., Laszlo V., Helbich T.H., Hegedus B., Klikovits T., Hoda M.A., Klepetko W., Paku S., Marko-Varga G, & Dome B. (2017). Limited Tumor Tissue Drug Penetration Contributes to Primary Resistance against Angiogenesis Inhibitors. Theranostics, 7(2), 400-412.

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MALDI-MS Structure Elucidation Protocol

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For structure elucidation MALDI-analysis, samples were mixed 1∶2 with 1 µl of a 20 mM 4-chloro-α-cyanocinnamic acid (ClCCA) in 70% ACN with 0.1% trifluoracetic acid (TFA) or 9-aminoacridin in acetone, spotted onto a polished stainless steel target and air-dried. MALDI-MS analysis was performed with a MALDI LTQ Orbitrap XL (Thermo Fisher Scientific, Inc., Waltham, MA) equipped with a nitrogen laser at 337 nm as described previously [25] (link)–[26] (link). Qual Browser (version 2.0.7; Thermo Fisher Scientific, Inc., Waltham, MA) was used for spectra analysis and to calculate possible sum formulas.

Schöner T.A., Fuchs S.W., Reinhold-Hurek B, & Bode H.B. (2014). Identification and Biosynthesis of a Novel Xanthomonadin-Dialkylresorcinol-Hybrid from Azoarcus sp. BH72. PLoS ONE, 9(3), e90922.

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MALDI-MSI Protocol for Metabolomic Analysis

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A MALDI LTQ-Orbitrap XL hybrid mass spectrometer (Thermo Fisher Scientific, Bremen, Germany) equipped with a nitrogen laser (337 nm, rep. rate = 60 Hz, spot size = 80 × 120 μm) was used for mass analysis. The instrument was externally calibrated using commercial peptide standard mixtures (ProteoMass calibration kit, Sigma-Aldrich) for either the normal (m/z 150–2,000) or high (m/z 200–4,000) mass range. Xcalibur (version 2.3) from Thermo Fisher Scientific was used for MALDI-MSI data acquisition in positive and negative ion mode. The ion mass range was set to 400–1,000 Da in positive ion mode and 750–2,000 in negative ion mode, with 10 laser shots per step at laser energy of 15 μJ. The target plate stepping distance was set to 100 μm for both the x- and y-axes. The mass resolution was 100,000 (full width at half maximum at m/z 400).

Drescher H.K., Weiskirchen R., Fülöp A., Hopf C., de San Román E.G., Huesgen P.F., de Bruin A., Bongiovanni L., Christ A., Tolba R., Trautwein C, & Kroy D.C. (2019). The Influence of Different Fat Sources on Steatohepatitis and Fibrosis Development in the Western Diet Mouse Model of Non-alcoholic Steatohepatitis (NASH). Frontiers in Physiology, 10, 770.

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MALDI-MSI Sample Preparation for Medicago Nodules

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Sample preparation for MALDI-MSI is a critical step to obtain the best results during the MALDI-MSI analysis. Sample preparation steps, such as sample preservation, washing, matrix choice, and matrix application method will all influence the sample analysis. Here, we describe sample preparation steps for flash freezing the nodules and embedding in gelatin, followed by matrix application with a TM Sprayer automatic sprayer system (HTX Technologies). The sample is analyzed on the MALDI LTQ Orbitrap XL (Thermo Scientific) equipped with a nitrogen laser, and data analysis is performed in ImageQuest (Thermo Scientific) and MSiReader [18 (link)]. Figure 1 demonstrates the sample workflow for MALDI-MSI of Medicago root nodules.

Keller C., Gemperline E, & Li L. (2020). MALDI Mass Spectrometry Imaging of Peptides in Medicago Truncatula Root Nodules. Methods in molecular biology (Clifton, N.J.), 2139, 341-351.

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On-Tissue Budesonide Detection via MSI

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Budesonide is challenging to detect by MSI as it is not easily protonated or deprotonated. Therefore, to improve the detection of budesonide in lung tissue sections, an on-tissue chemical derivatization protocol was adopted as recently described by Zecchi et al. [16 (link)]. Briefly, this approach uses GirP as an on tissue derivatizing agent, followed by FA matrix coating. After coating, samples were finally dried in a vacuum desiccator for 15 min. Acquisition was performed on a vacuum MALDI-LTQ-Orbitrap XL mass spectrometer (Thermo Fisher, San Josè, CA, USA) using a raster size of 400 × 400 µm in the mass range from m/z 185 to 650 in full scan positive ion mode. 2D ion intensity maps were created by plotting the intensity of budesonide-GirP molecular ion (564.308 m/z). Signal normalization was performed by using the derivatized triamcinolone ion (568.283 m/z). All ion traces were extracted with a tolerance of 0.005 Da.

Zecchi R., Franceschi P., Tigli L., Pioselli B., Mileo V., Murgia X., Salomone F., Pieraccini G., Usada H., Schmidt A.F., Hillman N.H., Kemp M.W, & Jobe A.H. (2021). Surfactant-Assisted Distal Pulmonary Distribution of Budesonide Revealed by Mass Spectrometry Imaging. Pharmaceutics, 13(6), 868.

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Evaluating PZA Concentration in TB Lesions

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Two rabbits were infected as described above, and disease was allowed to progress for 11 wk, at which point the rabbits received a single dose of PZA at 300 mg/kg (a higher dose was used than in efficacy studies to overcome the relatively poor ionization of PZA by MALDI-MSI), after which lesions and the surrounding lung tissue were collected 2 h postdose and stored as described previously (Zimmerman et al., 2017 (link)). 12-µm-thick tissue sections were prepared from γ-irradiated biopsies for MALDI-MSI and analyzed by using a MALDI LTQ Orbitrap XL mass spectrometer (Thermo Fisher Scientific) as previously described (Prideaux et al., 2015 (link)). Serial 25- and 12-µm-thick sections were prepared for LCM coupled to high-pressure liquid chromatography and tandem mass spectrometry quantitative analysis, and H&E staining respectively. Microdissection and quantification of caseum, cellular lesion, and uninvolved lung were performed as previously described (Zimmerman et al., 2017 (link)).

Blanc L., Sarathy J.P., Alvarez Cabrera N., O’Brien P., Dias-Freedman I., Mina M., Sacchettini J., Savic R.M., Gengenbacher M., Podell B.K., Prideaux B., Ioerger T., Dick T, & Dartois V. (2018). Impact of immunopathology on the antituberculous activity of pyrazinamide. The Journal of Experimental Medicine, 215(8), 1975-1986.

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MALDI-MSI of Human Skin Samples

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All MSI analysis of human skin samples on NAPA was performed using a MALDI-LTQ-Orbitrap XL mass spectrometer (Thermo Scientific, San Jose, CA). A nitrogen laser emitting radiation at 337 nm with a focal spot size of ~100 µm × 80 µm was operated at a laser fluence of ~150 mJ/cm² with 3 laser shots/scan and a raster step size of 100 µm. All mass spectra were acquired from m/z 180 and 1,000 using the orbitrap mass analyzer at a mass resolving power setting of 30,000. After acquisition, all MS images were generated with a m/z tolerance of 5 mDa using the ImageQuest software package (Thermo Scientific). Ion images were smoothed using the linear function.

Fincher J.A., Jones D.R., Korte A.R., Dyer J.E., Parlanti P., Popratiloff A., Brantner C.A., Morris N.J., Pirlo R.K., Shanmugam V.K, & Vertes A. (2019). Mass Spectrometry Imaging of Lipids in Human Skin Disease Model Hidradenitis Suppurativa by Laser Desorption Ionization from Silicon Nanopost Arrays. Scientific Reports, 9, 17508.

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MALDI-LTQ-Orbitrap XL Mass Spectrometry

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All MS experiments were performed on a MALDI-LTQ-Orbitrap XL mass spectrometer (Thermo Scientific, Bremen, Germany) equipped with 60 Hz 337 nm N₂ laser. Full scan mass resolution of 60,000 (at m/z 400), laser energy of 18 μJ and microscans of 4 were used for all analyses. MS/MS were performed in HCD mode with normalized collision energies of 45 and isolation window of 3 m/z (unless otherwise stated). Monoisotopic precursor selection was enabled. Different dynamic exclusion durations were tested and optimized. The multiplex MS imaging method was set up in Xcalibur software (Thermo Scientific, Bremen, Germany) and the imaging position file was defined in TunePlus software (Thermo Scientific, Bremen, Germany).

OuYang C., Chen B, & Li L. (2015). High throughput in situ DDA analysis of neuropeptides by coupling novel multiplex mass spectrometric imaging (MSI) with gas phase fractionation. Journal of the American Society for Mass Spectrometry, 26(12), 1992-2001.

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Cryo-MALDI-MSI of Desiccated Seeds

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Mature desiccated seeds of two accessions were embedded in a 10% gelatin solution, frozen and cryo-sectioned as described previously (Sturtevant et al., 2015 (link)). Tissue sections were coated with 2, 5-dihydroxybenzoic acid (DHB; 98%, Sigma-Aldrich) by sublimation, following the method adapted from Hankin et al. (2007) (link). Coated seed sections were analyzed by a hybrid MALDI-linear ion trap-Orbitrap mass spectrometer (MALDI-LTQ-Orbitrap XL; Thermo Scientific, San Jose, CA, USA) as described by Lu et al. (2018) (link). MALDI-MSI data analysis and images processing were performed according to the method described by Horn and Chapman (2014b) (link).

Lu S., Aziz M., Sturtevant D., Chapman K.D, & Guo L. (2020). Heterogeneous Distribution of Erucic Acid in Brassica napus Seeds. Frontiers in Plant Science, 10, 1744.

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