OCT 24, 2018 12:00 PM PDT

Ion Mobility-Mass Spectrometry in the -Omics

C.E. Credits: P.A.C.E. CE Florida CE
Speakers
  • Assistant Professor of Chemistry, Department of Biomedical and Chemical Engineering and Sciences (BCES), Florida Institute of Technology
    Biography
      Dr. Chouinard was born and raised in the small town of Grafton, MA. His interests in chemistry and biology brought him south, where he attended University of North Carolina at Chapel Hill (Go Tar Heels!) and furthered his passion for analytical chemistry. After briefly working as a project manager for a contract research lab back in Massachusetts, Chris pursued his Ph.D. at the University of Florida. There, Chris worked under world renowned mass spectrometrist Rick Yost, and was responsible for integrating drift tube-ion mobility spectrometry (DTIMS) into the Yost lab. Chris's interests at UF involved IM-MS studies of clinical molecules (steroids, Vitamin D metabolites) and he also received grant funding through the Partnership for Clean Competition to develop novel IM-MS methods for improved identification of anabolic androgenic steroids in athletes.

      After graduating from UF, Chris traveled to the opposite corner of the country to engage in a prestigious post-doctoral position at Pacific Northwest National Laboratory (PNNL) in Richland, WA. While working with Dick Smith, another world leader in mass spectrometry, Chris designed and developed a Structures for Lossless Ion Manipulations (SLIM) platform that enabled the first integration of LC into the SLIM IM-MS pipeline for improved analysis in phosphoproteomics.

      Chris joined the faculty at Florida Tech in the summer of 2018 and will continue his work in ion mobility-mass spectrometry. Current projects involve improved methods for metabolomics and lipidomics with gas-phase chemistry.

    Abstract:

    Ion mobility-mass spectrometry (IM-MS) is a rapid, gas-phase separation technique that has become an integral part of the analytical repertoire of techniques for the -omics. This method couples well with existing protocols (i.e., LC-MS) by affording an additional dimension of separation, and provides a characteristic measure of an analyte’s size, shape, and charge in the form of a collision cross section (CCS). CCS can be used to increase confidence in quantitative measurement of known compounds, thus reducing interferences and improving S:N ratios, and also serves as a defining feature in identification of unknowns. Furthermore, this separation based on structure (as opposed to mass-to-charge alone) allows for distinction of structural and stereoisomers of potential biological importance.

    This presentation will cover the basic operating principles of IMS and current instrumentation; applications to metabolomics, lipidomics, and proteomics; and future directions for IM-MS, such as implementation in routine clinical analysis.

    Learning Objectives: 

    1. Understand the basic operating principles of IMS and current instrumentation
    2. Understand current applications to metabolomics, lipidomics, and proteomics


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