Final Report - Advanced Ion Trap Mass Spectrometry Program - Oak Ridge National Laboratory - Sandia National Laboratory

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This report covers the three main projects that collectively comprised the Advanced Ion Trap Mass Spectrometry Program. Chapter 1 describes the direct interrogation of individual particles by laser desorption within the ion trap mass spectrometer analyzer. The goals were (1) to develop an ''intelligent trigger'' capable of distinguishing particles of biological origin from those of nonbiological origin in the background and interferent particles and (2) to explore the capability for individual particle identification. Direct interrogation of particles by laser ablation and ion trap mass spectrometry was shown to have good promise for discriminating between particles of biological origin and those ... continued below

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Whitten, W.B. December 18, 2002.

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Description

This report covers the three main projects that collectively comprised the Advanced Ion Trap Mass Spectrometry Program. Chapter 1 describes the direct interrogation of individual particles by laser desorption within the ion trap mass spectrometer analyzer. The goals were (1) to develop an ''intelligent trigger'' capable of distinguishing particles of biological origin from those of nonbiological origin in the background and interferent particles and (2) to explore the capability for individual particle identification. Direct interrogation of particles by laser ablation and ion trap mass spectrometry was shown to have good promise for discriminating between particles of biological origin and those of nonbiological origin, although detailed protocols and operating conditions were not worked out. A library of more than 20,000 spectra of various types of biological particles has been assembled. Methods based on multivariate analysis and on neural networks were used to discriminate between particles of biological origin and those of nonbiological origin. It was possible to discriminate between at least some species of bacteria if mass spectra of several hundred similar particles were obtained. Chapter 2 addresses the development of a new ion trap mass analyzer geometry that offers the potential for a significant increase in ion storage capacity for a given set of analyzer operating conditions. This geometry may lead to the development of smaller, lower-power field-portable ion trap mass spectrometers while retaining laboratory-scale analytical performance. A novel ion trap mass spectrometer based on toroidal ion storage geometry has been developed. The analyzer geometry is based on the edge rotation of a quadrupolar ion trap cross section into the shape of a torus. Initial performance of this device was poor, however, due to the significant contribution of nonlinear fields introduced by the rotation of the symmetric ion-trapping geometry. These nonlinear resonances contributed to poor mass resolution and sensitivity and to erratic ion ejection behavior. To correct for these nonlinear effects, the geometry of the toroid ion trap analyzer has been modified to create an asymmetric torus, as first suggested by computer simulations that predicted significantly improved performance and unit mass resolution for this geometry. A reduced-sized version (one-fifth scale) has been fabricated but was not tested within the scope of this project. Chapter 3 describes groundbreaking progress toward the use of ion-ion chemistry to control the charge state of ions formed by the electrospray ionization process, which in turn enables precision analysis of whole proteins. In addition, this technique may offer the unique possibility of a priori identification of unknown biological material when employed with existing proteomics and genomic databases. Ion-ion chemistry within the ion trap was used to reduce the ions in highly charged states to states of +1 and +2 charges. Reduction in charge greatly simplifies identification of molecular weights of fragments from large biological molecules. This technique enables the analysis of whole proteins as biomarkers for the detection and identification of all three classes of biological weapons (bacteria, toxins, and viruses). In addition to methods development, tests were carried out with samples of tap water, local creek water, and soil (local red clay) spiked with melittin (bee venom), cholera toxin, and virus MS2. All three analytes were identified in tap water and soil; however, all three were problematic for detection in creek water at concentrations of 1 nM. More development of methods is needed.

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  • Report No.: ORNL/TM-2002/215
  • Grant Number: DE-AC05-00OR22725
  • DOI: 10.2172/885641 | External Link
  • Office of Scientific & Technical Information Report Number: 885641
  • Archival Resource Key: ark:/67531/metadc892143

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  • December 18, 2002

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  • Sept. 23, 2016, 2:42 p.m.

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  • Dec. 8, 2016, 7:15 p.m.

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Whitten, W.B. Final Report - Advanced Ion Trap Mass Spectrometry Program - Oak Ridge National Laboratory - Sandia National Laboratory, report, December 18, 2002; [Tennessee]. (digital.library.unt.edu/ark:/67531/metadc892143/: accessed November 18, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.