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Mass Spectrometry Webinars - Live and on-Demand

Bruker Webinars - tune in and get the latest insights about new technologies, scientific developments, innovative analytical methods and catch late-breaking news.

If you were unable to attend the live webinars, or if you would like to view it again, you can view the on-demand version at your convenience. Registration is required to participate in live webinars or view the recordings of on-demand webinars.


11 am (EDT) /
17 pm (CET)
Rapid and Sensitive Quantitation of Approximately 100 Synthetic Cannabinoids In Serum by UHPLC-Triple Quadrupole Mass Spectrometry

Presenters: Rafaela Martin, PhD, Applications Specialist, Bruker Daltonics

The term synthetic cannabinoid refers to an increasing number of man-made mind-altering chemicals that are sprayed on dried, shredded plant material so they can be smoked, or sold as liquids to be vaporized and inhaled in e-cigarettes and other devices. Because of their similarity to compounds found in the marijuana plant, these chemicals are misleadingly called synthetic marijuana to circumvent current legislation and routine drug testing methods. They are then unscrupulously marketed as safe and legal, despite the fact that their effects can be unpredictable, often leading to severe or even life-threatening conditions. In order to keep ahead of evolving drug prohibition laws, new or slightly modified variants (analogues) of synthetic cannabinoids are regularly synthesized and marketed to the recreational drug user market.
In this webinar, we describe the application of UHPLC-triple quadrupole mass spectrometry using multiple reaction monitoring (MRM) to rapidly and reliably quantify approximately 100 synthetic cannabinoids in human serum at the low ng/mL level.

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11 am (EST)
Uncovering Metabolic Pathways in Disease to Support Drug Discovery Using High Resolution MALDI Imaging Mass spectrometry

Presenters: Ellen Jones, Ph.D., MALDI Imaging Research Center, Genentech; Dr. Dennis Trede, Ph.D., Managing Director, SciLS Bremen

Matrix assisted laser desorption ionization imaging mass spectrometry (MALDI-IMS) is a robust, label free tool to produce ion-density maps representing the distribution of a variety of analytes within a tissue section of interest. Incorporation of high-resolution FTICR (Fourier transform ion cyclotron resonance) mass spectrometers into existing workflows has now allowed for simultaneous detection of drug and downstream pharmacodynamic responses in a single acquisition. This approach was recently utilized to assess the effects of a drug compound known to elicit a PD response targeting the tryptophan pathway. Whole body tissue sections derived from tumor bearing mice dosed with drug or vehicle were analyzed using MALDI FTICR IMS to evaluate the tissue distribution of tryptophan metabolites. Tissues were sectioned and analyzed in positive ion mode, where 21/24 of the nodes of the pathway could be identified. Two central nodes of the tryptophan metabolism pathway, tryptophan and kynurenine were found to have a pharmacodynamic response to dosing, with tryptophan increasing and kynurenine decreasing in tumors, a finding validated not only by MALDI-IMS but also a complimentary quantitative LC-MS/MS assay. Following the success of the tryptophan study, method development to image additional key metabolic pathways, such as the TCA cycle are ongoing. Preliminary data from these efforts will be presented, along with 3D images representing the first feasibility study to confirm that 3D volume reconstruction is achievable using data collected on an FTICR mass spectrometer. The 3D imaging study was made possible using new acquisition software from Bruker Daltonics and 3D reconstruction software from SCiLS version 2015a (Bremen, Germany). A variety of lipid species including phosphatidylcholines and sphingomyelins were identified across a 3D volume in this pilot project and will be displayed, highlighting the potential impact 3D imaging studies may have in metabolomics workflows, specifically in studies involving heterogeneous tissues such as tumors..

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16 pm (CEST)
Structure Elucidation with Trapped Ion Mobility Spectrometry

Presenters: Dr. Christian Bleiholder, Ph.D., Assistant Professor of Chemistry & Biochemistry, Florida State University

Ion mobility spectrometry - mass spectrometry (IMS-MS) offers great potential to structurally characterize biological macromolecules and their complexes, ranging from amyloid assemblies to viral capsids and allosteric control of protein function. Trapped ion mobility spectrometry (TIMS) is a novel ion mobility method with unique capabilities for structural studies. One unique feature of TIMS is the ability to trap ions for extended periods of time. Further, TIMS has demonstrated unparalleled ion mobility separation power.
This webinar will discuss the technical and theoretical foundation of TIMS, demonstrate the capabilities of TIMS in terms of its resolving power and ability to trap ions for extended periods of time, and illustrate its potential for structural biology studies in conjunction with novel computational methods.

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