Thermo Scientific Exactive Plus Benchtop Full-Scan Orbitrap Mass
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Simultaneous Analysis of Drugs in Forensic Cases by Liquid Chromatography–High‑Resolution Orbitrap Mass Spectrometry
Chromatographia (2020) 83:53–64 https://doi.org/10.1007/s10337-019-03814-w ORIGINAL Simultaneous Analysis of Drugs in Forensic Cases by Liquid Chromatography–High‑Resolution Orbitrap Mass Spectrometry Siti U. Mokhtar1 · Chadin Kulsing2,3,4 · Jalal T. Althakafy2,5 · Alex Kotsos6 · Olaf H. Drummer6,7 · Philip J. Marriott2 Received: 10 May 2019 / Revised: 23 September 2019 / Accepted: 15 October 2019 / Published online: 31 October 2019 © Springer-Verlag GmbH Germany, part of Springer Nature 2019 Abstract In the present study, liquid chromatography coupled to an Orbitrap mass spectrometer (HPLC–Q-Orbitrap MS) was used as an approach for identifcation and quantifcation of 113 drugs simultaneously in biological samples (whole blood/plasma/ serum). Samples were prepared using liquid–liquid extraction conducted using a trizma/isopropanol/butyl chloride bufer system. Reversed-phase separation employing a column (50 × 2.1 mm) packed with 2.6-μm C18 particles was then performed under gradient elution with mobile phase composition consisting of acetic acid and aqueous-acetonitrile mixtures with the acetonitrile content ranging from 10 to 100% v/v. Compounds were detected with high-resolution MS operated in full scan mode having a mass accuracy < 5 ppm. In this study, isobaric compounds (same nominal mass) were easily distinguished and identifed by their diferent retention times. Extracted ion chromatograms (XICs) with narrow mass tolerance window (5 ppm) 2 provided analysis with acceptable linearity (r ) ranged from 0.9530 to 1, low limits of detection (LOD) (0.02–39 ng mL−1) and low limit of quantifcation (LOQ) (0.1–130 ng mL−1). The developed method was applied to successfully analyse drugs in 26 blood samples from positive forensic cases and proved that this technique was able to detect analytes at trace level. -
ADVANCED SPECTROMETER Introduction
ADVANCED SPECTROMETER Introduction In principle, a spectrometer is the simplest of scientific very sensitive detection and precise measurement, a real instruments. Bend a beam of light with a prism or diffraction spectrometer is a bit more complicated. As shown in Figure grating. If the beam is composed of more than one color of 1, a spectrometer consists of three basic components; a light, a spectrum is formed, since the various colors are collimator, a diffracting element, and a telescope. refracted or diffracted to different angles. Carefully measure The light to be analyzed enters the collimator through a the angle to which each color of light is bent. The result is a narrow slit positioned at the focal point of the collimator spectral "fingerprint," which carries a wealth of information lens. The light leaving the collimator is therefore a thin, about the substance from which the light emanates. parallel beam, which ensures that all the light from the slit In most cases, substances must be hot if they are to emit strikes the diffracting element at the same angle of inci- light. But a spectrometer can also be used to investigate cold dence. This is necessary if a sharp image is to be formed. substances. Pass white light, which contains all the colors of The diffracting element bends the beam of light. If the beam the visible spectrum, through a cool gas. The result is an is composed of many different colors, each color is dif- absorption spectrum. All the colors of the visible spectrum fracted to a different angle. are seen, except for certain colors that are absorbed by the gas. -
Spectrum 100 Series User's Guide
MOLECULAR SPECTROSCOPY SPECTRUM 100 SERIES User’s Guide 2 . Spectrum 100 Series User’s Guide Release History Part Number Release Publication Date L1050021 A October 2005 Any comments about the documentation for this product should be addressed to: User Assistance PerkinElmer Ltd Chalfont Road Seer Green Beaconsfield Bucks HP9 2FX United Kingdom Or emailed to: [email protected] Notices The information contained in this document is subject to change without notice. Except as specifically set forth in its terms and conditions of sale, PerkinElmer makes no warranty of any kind with regard to this document, including, but not limited to, the implied warranties of merchantability and fitness for a particular purpose. PerkinElmer shall not be liable for errors contained herein for incidental consequential damages in connection with furnishing, performance or use of this material. Copyright Information This document contains proprietary information that is protected by copyright. All rights are reserved. No part of this publication may be reproduced in any form whatsoever or translated into any language without the prior, written permission of PerkinElmer, Inc. Copyright © 2005 PerkinElmer, Inc. Trademarks Registered names, trademarks, etc. used in this document, even when not specifically marked as such, are protected by law. PerkinElmer is a registered trademark of PerkinElmer, Inc. Spectrum, Spectrum 100, and Spectrum 100N are trademarks of PerkinElmer, Inc. Spectrum 100 Series User’s Guide . 3 Contents Contents............................................................................................... -
Mass Spectrometer Business Presentation Materials
Mass Spectrometer Business Presentation Materials Hiroto Itoi, Corporate Officer Deputy General Manager of the Analytical & Measuring Instruments Division Shimadzu Corporation Jul. 3, 2018 Contents I. Introduction • Expansion of Mass Spectrometry ………………………………………………………………… p.3 • History of Shimadzu's Growth in Mass Spectrometry …………………………………………… p.5 II. Overview of Mass Spectrometers • Operating Principle, Demand Trends, and Vendors ……………………………………………… p.9 • Mass Spectra ………………………………………………………………………………………… p.10 • Configuration of Mass Spectrometers …………………………………………………………… p.11 • Ionization …………………………………………………………………………………………… p.12 • Mass Separation …………………………………………………………………………………… p.14 III. Shimadzu's Mass Spectrometer Business • Product Type ………………………………………………………………………………………… p.17 • Application Software ………………………………………………………………………………… p.18 • Growth Strategy for Mass Spectrometer Business ……………………………………………… p.19 • Expand/Improve Product Lines …………………………………………………………………… p.20 • Measures to Expand Application Fields …………………………………………………………… p.24 • Measures to Automate Data Processing Using AI ……………………………………………… p.25 IV. Summary • Future Direction ……………………………………………………………………………………… p.26 July 2018 Mass Spectrometer Business Presentation Materials 2 I. Introduction Expansion of Mass Spectrometry (1) Why Mass Spectrometry? Mass spectrometry is able to analyze a wide variety of compounds with high accuracy and high efficiency (simultaneous multicomponent analysis). It offers superior characteristics that are especially beneficial in the following fields, -
Advantages of the LTQ Orbitrap for Protein Identification in Complex Digests
Application Note: 386 Advantages of the LTQ Orbitrap for Protein Identification in Complex Digests Rosa Viner, Terry Zhang, Scott Peterman, and Vlad Zabrouskov, Thermo Fisher Scientific, San Jose, CA, USA Introduction Materials and Methods Key Words Comprehensive, accurate identification of proteins in Sample Preparation • LTQ Orbitrap complex sample mixtures is an important fundamental capability for any proteomics research laboratory. Technology Ten µL of E. coli cell lysate diluted 20-fold with 6 M • Peptide advancements in both hardware and software continue to guanidine HCl in 50 mM ammonium bicarbonate (pH 8.0) Sequencing expand and refine our view of any proteomic system in was reduced with 5 mM DTT, alkylated with 25 mM iodoacetic acid and digested at 37 °C for 16 hours. • Protein terms of protein identities and their post-translational Identification modifications (PTMs). It has been suggested that the very HPLC recent ability to routinely obtain accurate mass measurements Column: C18 Packed tip, 75 µm x 75 mm (QSTAR Elite); • PTMs (< 5 ppm RMS) on precursor and MS/MS fragment ions C18 column, 75 µm x 100 mm (LTQ Orbitrap XL) in proteomic experiments should lead to unprecedented Mobile phase A: 0.1% Formic Acid in Water with accuracy in the ability to identify and characterize proteins.1 2% Acetonitrile This paper compares alternative approaches to this Mobile phase B: 0.1% Formic Acid in Acetonitrile challenging application using two high performance Flow Rate: 300 nL/min platforms for proteomics: a QqTOF instrument (QSTAR® Gradient: 5% B to 35% B in 90 min Elite from Applied Biosystems) and a hybrid linear ion trap- orbitrap instrument (Thermo Scientific LTQ Orbitrap XL). -
Experiment 2 Radiation in the Visible Spectrum Emission Spectra Can Be
Experiment 2 Radiation in the Visible Spectrum Emission spectra can be a unique fingerprint of an atom or molecule. The photon energies and wavelengths are directly related to the allowed quantum energy states of the system. In the following experiments we will examine the radiation given off by sources radiating in the visible region. We will be using a spectrometer produced by Ocean Optics. Light enters the spectrometer via a fiber optic cable. Inside the spectrometer a diffraction grating diffracts the different frequencies onto a CCD. The CCD basically ”counts” the photons according to wavelength. The data is transferred via a usb port to a PC. The Ocean Optics software displays the spectrum as counts versus wavelength. We will examine the spectra given off by the following sources: incandescent light filament, hydrogen, helium, various light emitting diodes and a laser pointer. You will also be given an unknown gas discharge tube and will need to identify the gas via its spectral emissions Pre Lab 1) Obtain a spectrum for hydrogen, mercury, sodium and neon gas emissions. The spectrum must contain an accurate listing of major emission lines (in nm), not simply a color photo of the emission. 2) Make yourself familiar with the manual for the spectrometer and the software. These are available via the following links: http://www.oceanoptics.com/technical/hr4000.pdf http://www.oceanoptics.com/technical/SpectraSuite.pdf These documents are also available on Black Board. 3) How does the Ocean Optics spectrometer work? In your answer list its three main components and describe what each component does. -
Orbitrap Fusion Tribrid Mass Spectrometer
MASS SPECTROMETRY Product Specifications Thermo Scientific Orbitrap Fusion Tribrid Mass Spectrometer Unmatched analytical performance, revolutionary MS architecture The Thermo Scientific™ Orbitrap Fusion™ mass spectrometer combines the best of quadrupole, Orbitrap, and linear ion trap mass analysis in a revolutionary Thermo Scientific™ Tribrid™ architecture that delivers unprecedented depth of analysis. It enables life scientists working with even the most challenging samples—samples of low abundance, high complexity, or difficult-to-analyze chemical structure—to identify more compounds faster, quantify them more accurately, and elucidate molecular composition more thoroughly. • Tribrid architecture combines quadrupole, followed by ETD or EThCD for glycopeptide linear ion trap, and Orbitrap mass analyzers characterization or HCD followed by CID • Multiple fragmentation techniques—CID, for small-molecule structural analysis. HCD, and optional ETD and EThCD—are available at any stage of MSn, with The ultrahigh resolution of the Orbitrap mass subsequent mass analysis in either the ion analyzer increases certainty of analytical trap or Orbitrap mass analyzer results, enabling molecular-weight • Parallelization of MS and MSn acquisition determination for intact proteins and confident to maximize the amount of high-quality resolution of isobaric species. The unsurpassed data acquired scan rate and resolution of the system are • Next-generation ion sources and ion especially useful when dealing with complex optics increase system ease of operation and robustness and low-abundance samples in proteomics, • Innovative instrument control software metabolomics, glycomics, lipidomics, and makes setup easier, methods more similar applications. powerful, and operation more intuitive The intuitive user interface of the tune editor The Orbitrap Fusion Tribrid MS can perform and method editor makes instrument calibration a wide variety of analyses, from in-depth and method development easier. -
Mass Spectrometer
CLASSICAL CONCEPT REVIEW 6 Mass Spectrometer One of several devices currently used to measure the charge-to-mass ratio q m of charged atoms and molecules is the mass spectrometer. The mass spectrometer is used to find the charge-to-mass ratio of ions of known charge by measuring> the radius of their circular orbits in a uniform magnetic field. Equation 3-2 gives the radius of R for the circular orbit of a particle of mass m and charge q moving with speed u in a magnetic field B that is perpendicular to the velocity of the particle. Figure MS-1 shows a simple schematic drawing of a mass spectrometer. Ions from an ion source are accelerated by an electric field and enter a uniform magnetic field produced by an electromagnet. If the ions start from rest and move through a poten- tial DV, their kinetic energy when they enter the magnetic field equals their loss in potential energy, qDV: B out 1 mu2 = qDV MS-1 2 R The ions move in a semicircle of radius R given by Equation 3-2 and exit through a P P narrow aperture into an ion detector (or, in earlier times, a photographic plate) at point 1 u 2 P2, a distance 2R from the point where they enter the magnet. The speed u can be eliminated from Equations 3-2 and MS-1 to find q m in terms of DV, B, and R. The + + q result is Source > – + q 2DV ∆V = 2 2 MS-2 m B R MS-1 Schematic drawing of a mass spectrometer. -
High Resolution LC-MS for Screening and Quantitative
High Resolution LC-MS for Screening and Quantitative Analysis of Antibiotics in Drinking Water Using an Orbitrap and Online Sample Preparation Jonathan Beck, Charles Yang, Dipankar Ghosh, Kristi Akervik; Thermo Fisher Scientific, San Jose, CA, USA Mass Spectrometry TABLE 2. List of antibiotics analyzed with their theoretical masses, LOQs and FIGURE 4. Spectral comparision of the MS2 spectrum of the antibiotic Overview Results reproducibility trimethoprim obtained at a concentration of 80 pg/mL. The library reference The Exactive™ Plus Orbitrap mass spectrometer was used in this experiment. The spectrum is the top spectrum, the lower spectrum is from the sample. The Purpose: To demonstrate online sample pre-concentration and extraction of water Exactive Plus was operated in alternating full scan and all ion fragmentation (AIF) Quantitation Compound Theoretical Mass (m/z) LOQ (pg/mL) % RSD at LOQ samples and analysis with high-resolution, accurate mass (HR/AM) detection, comparison was performed with ExactFinder software. mode with positive electrospray ionization. One scan of full scan MS data was Acquisition and quantitation was carried out using TraceFinder™ software. The Carbamazepine 332.14050 0.2 8.90 quantitation and confirmation. collected, and subsequently, all of the ions entering the MS were fragmented in the theoretical mass of each protonated antibiotic compound was used as the mass for Erythromycin 734.46852 40.0 14.30 Methods: Inject 1 mL water samples directly onto a trapping column. The trapped higher-energy C-trap dissociation (HCD) collision cell at a collision energy (CE) of quantitation in this analysis. Calibration lines were created for each compound, and fit Ketoprofen 255.10157 1.0 9.90 compounds are then backflushed onto an analytical HPLC column and detected using 30 eV with a 20% stepped CE, and analyzed in the Orbitrap mass analyzer. -
A Novel High Resolution Accurate Mass Orbitrap-Based GC-MS
ROUTINE OR RESEARCH GC-Orbitrap for Environmental Analysis a collaboration between ROUTINE OR RESEARCH GC-Orbitrap for Environmental Analysis Foreword A Novel High Resolution Accurate Mass Orbitrap-based GC-MS Platform for Routine Analysis of Short Chained Chlorinated Paraffins In this study, the performance of a novel bench top, high resolution accurate mass Orbitrap™-based GC-MS was tested for the analysis of SCCPs. System performance was tested using full-scan acquisition and simple instrumental setup. Pyrolysis-GC-Orbitrap MS - A Powerful Analytical Tool for Identification and Quantification of Microplastics in a Biological Matrix The purpose of the experiments described in this work was to assess the applicability of pyrolysis-gas chromatography-Orbitrap™ mass spectrometry for the qualitative and quantitative analysis of plastic polymers in complex biological matrices. Low Level Quantification of NDMA and Non-targeted Contaminants Screening in Drinking Water using GC Orbitrap Mass Spectrometry In this work, a sensitive and selective method for NDMA detection and quantification using high resolution accurate mass GC Orbitrap™ technology is described. Overcoming Analytical Challenges for Polybrominated Diphenyl Ethers (PBDEs) Analysis in Environmental Samples using Gas Chromatography – Orbitrap Mass Spectrometry The note demonstrates the quantitative performance of the Thermo Scientific™ Exactive™ GC Orbitrap™ GC-MS mass spectrometer for the analysis of polybrominated diphenyl ethers (PBDEs) in environmental samples. Versatility of GC-Orbitrap Mass Spectrometry for the Ultra-trace Detection of Persistent Organic Pollutants in Penguin Blood from Antarctica In this study, the performance of the Thermo Scientific™ Q Exactive™ GC Orbitrap™ mass spectrometer was evaluated for routine analysis of POPs within King penguin blood from Antarctica. -
Development and Applications of a Real-Time Magnetic Electron
Louisiana State University LSU Digital Commons LSU Doctoral Dissertations Graduate School 12-13-2017 Development and Applications of a Real-time Magnetic Electron Energy Spectrometer for Use with Medical Linear Accelerators Paul Ethan Maggi Louisiana State University and Agricultural and Mechanical College, [email protected] Follow this and additional works at: https://digitalcommons.lsu.edu/gradschool_dissertations Part of the Health and Medical Physics Commons Recommended Citation Maggi, Paul Ethan, "Development and Applications of a Real-time Magnetic Electron Energy Spectrometer for Use with Medical Linear Accelerators" (2017). LSU Doctoral Dissertations. 4180. https://digitalcommons.lsu.edu/gradschool_dissertations/4180 This Dissertation is brought to you for free and open access by the Graduate School at LSU Digital Commons. It has been accepted for inclusion in LSU Doctoral Dissertations by an authorized graduate school editor of LSU Digital Commons. For more information, please [email protected]. DEVELOPMENT AND APPLICATIONS OF A REAL-TIME MAGNETIC ELECTRON ENERGY SPECTROMETER FOR USE WITH MEDICAL LINEAR ACCELERATORS A Dissertation Submitted to the Graduate Faculty of the Louisiana State University and Agricultural and Mechanical College in partial fulfillment of the requirements for the degree of Doctor in Philosophy in The Department of Physics and Astronomy by Paul Ethan Maggi B.S., California Polytechnic State University, San Luis Obispo, 2012 May 2018 ACKNOWLEDGEMENTS I thank Kenneth Hogstrom for providing the initial idea for this project, as well as partial funding support. I thank Edison Liang of Rice University for providing the magnet block and measurements of the magnetic field. I thank my adviser, Kip Matthews for his advice, guidance, and patience during my tenure at LSU. -
Peptide and Protein Quantification Using Itraq with Electron Transfer Dissociation
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Peptide and Protein Quantification Using iTRAQ with Electron Transfer Dissociation Doug Phanstiel,a Yi Zhang,c Jarrod A. Marto,c,d and Joshua J. a,bCoon a Department of Chemistry, University of Wisconsin, Madison, Wisconsin, USA b Department of Biomolecular Chemistry, University of Wisconsin, Madison, Wisconsin, USA c Department of Cancer Biology and Blais Proteomics Center, Dana-Farber Cancer Institute, Boston, Massachusetts, USA d Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA Electron transfer dissociation (ETD) has become increasingly used in proteomic analyses due to its complementarity to collision-activated dissociation (CAD) and its ability to sequence peptides with post-translation modifications (PTMs). It was previously unknown, however, whether ETD would be compatible with a commonly employed quantification technique, isobaric tags for relative and absolute quantification (iTRAQ), since the fragmentation mechanisms and pathways of ETD differ significantly from CAD. We demonstrate here that ETD of iTRAQ labeled peptides producesc- and z˙ -type fragment ions as well as reporter ions that are unique from those produced by CAD. Exact molecular formulas of product ions were determined by ETD fragmentation of iTRAQ-labeled synthetic peptides followed by high mass accuracy orbitrap mass analysis. These experiments revealed that ETD cleavage␣ of the N–C bond of the iTRAQ tag results in fragment ions that could be used for quantification. Synthetic peptide work demonstrates that these fragment ions provide up to three channels of quantification and that the quality is similar to that provided by beam-type CAD.