Speaker: Zachary Goecker, NIST

Topic: Developing Reproducible Methods in Site-Specific Glycosylation Analysis

Date: Monday, February 27, 2023

Time: 6:15 pm Dinner, 7:15 pm Presentation

Location: Shimadzu Scientific Instrument, Inc. Training Center 7100 Riverwood Drive, Columbia, MD 21046 (Directions)
This will be an in-person meeting. Attendees are required to show a vaccine card (either at the door or in advance using the web form) . If you have submitted your vaccine card before, your status is already recorded.

Dinner: Please RSVP to Andy Qi (andy.yue.qi@gmail.com) by Friday, February 24 if you will be attending the dinner.

Abstract: Many proteins are glycosylated at multiple sites, and each site can contain complex
distributions of attached glycans. Until recently, reliable determinations of these distributions have not been possible. Instead, glycosylation analysis of glycoproteins has been primarily accomplished by releasing and identifying glycans, thereby losing all protein site-specific information. This glycomics approach works well for understanding the diversity of glycosylation in a digest, but does not answer questions relevant to site-specific structures (glycan microheterogeneity) and therefore is not as useful in determining direct functional implications. Recent developments in high resolution mass spectrometry have opened the door for the identification of intact glycopeptides. This study assesses methods in site-specific analysis of intact glycopeptides to demonstrate
reproducibility and measure variation in glycosylation quantitatively between different experimental factors. Here, we report the use of stepped HCD fragmentation, contingent ion scan, and many downstream data filters for the production of highly robust and reproducible glycosylation distribution spectra. In this presentation, we will report site-specific glycosylation profiles on glycoproteins from Sars-Cov-2, influenza, blood serum, and breastmilk. Results demonstrate that glycosylation profiles are highly reproducible among replicates and different digestion methods. However, glycosylation patterns do change based on factors such as source, proteins sequence, and glycosylation site.

Thank you to our 2022-2023 sponsors!

Speaker: Jace Jones, University of Maryland School of Pharmacy

Topic: The Pursuit of How Structure Impacts Function: From Lipids to Oligonucleotides

Date: Monday, January 23, 2023

Time: 6:15 pm Dinner, 7:15 pm Presentation

Location: Shimadzu Scientific Instrument, Inc. Training Center 7100 Riverwood Drive, Columbia, MD 21046 (Directions)
This will be an in-person meeting. Attendees are required to show a vaccine card (either at the door or in advance using the web form) . If you have submitted your vaccine card before, your status is already recorded.

Dinner: Please RSVP to Andy Qi (andy.yue.qi@gmail.com) by Friday, January 20 if you will be attending the dinner.

Abstract: The functional role of a biological molecule hinges on its unique structure. The context by which structure impacts function is a vital piece of information that can
provide insight into underlying biological processes. One set of biological molecules that have received renewed interest for their biological significance and potential role as markers of cellular dysfunction are lipids. Cellular lipids have significant potential to inform on physiology owing to the pivotal role lipids play in many biological processes including cellular integrity, energy storage, and signaling pathways. In this presentation, I will share several examples of our multidimensional approach using separations (liquid and gas-phase), adduct consolidation, and mass spectrometry to characterize lipid structure. I will also present our recent progress on the lab’s effort to translate our analytical methods to the analysis of oligonucleotide therapeutics.

Thank you to our 2022-2023 sponsors!

Speaker: Stephen Valentine, West Virginia University

Topic: Developing Next-Generation Tools for Native Mass Spectrometry

Date: Monday, December 12, 2022

Time: 6:15 pm Dinner, 7:15 pm Presentation

Location: Shimadzu Scientific Instrument, Inc. Training Center 7100 Riverwood Drive, Columbia, MD 21046 (Directions)
This will be an in-person meeting. Attendees are required to show a vaccine card (either at the door or in advance using the web form) . If you have submitted your vaccine card before, your status is already recorded.

Dinner: Please RSVP to Andy Qi (andy.yue.qi@gmail.com) by Friday, December 9 if you will be attending the dinner.

Abstract: Native mass spectrometry (MS) is a powerful approach for structuralelucidation of large biomolecules. A number of technical and instrumental advances have enabled studies of diverse species ranging from protein machines to whole virus particles. However, biomolecules such as partially structured/unstructured proteins present a particular challenge to native MS. This presentation describes the development of new ionization technology with advantages in sensitivity and functionality for the study of these challenging molecules. The methods offer the best opportunity to study biomolecule conformer formation with broad implications for the study of disease processes and the development of therapeutics.

Thank you to our 2022-2023 sponsors!

Speaker: Nathan Basisty, National Institute on Aging, NIH

Topic: Uncovering Aging Mechanisms Through a Proteomic Lens: From Protein Turnover to Surfaceomes

Date: Monday, November 14, 2022

Time: 6:15 pm Dinner, 7:15 pm Presentation

Location: Shimadzu Scientific Instrument, Inc. Training Center 7100 Riverwood Drive, Columbia, MD 21046 (Directions)
This will be an in-person meeting. Attendees are required to show a vaccine card (either at the door or in advance using the web form) . If you have submitted your vaccine card before, your status is already recorded.

Dinner: Please RSVP to Andy Qi (andy.yue.qi@gmail.com) by Friday, November 11 if you will be attending the dinner.

Abstract: Mass spectrometry-based proteomics is a uniquely powerful tool to study basic mechanisms of aging. This talk will focus on how the Translational Geroproteomics Unit (NIA) leverages ‘geroproteomic’ approaches to develop biomarkers and therapeutic strategies against age related diseases stemming two major hallmarks of aging: loss of proteostasis and cellular senescence. Metabolic labeling studies have demonstrated that proteome turnover provides important insights into the biology of aging, however, measurement of whole animal turnover remains technically and computationally challenging. I will introduce a new freely available Skyline external tool, TurnoveR, that seamlessly integrates the computational pipeline analysis of protein turnover from metabolic labeling studies into the Skyline software environment. We hope this tool will facilitate the incorporation of protein turnover studies in the context of disease biology. Secondly, this talk will discuss how the Translational Geroproteomics Unit is leveraging secretome and surfaceome pipelines to develop strategies for quantifying and targeting pathogenic (senescent) cells that accumulate during aging to aid in the development of therapeutic against age-related diseases.

Speaker: Stephanie Cologna, University of Illinois Chicago

Topic: Mass Spectrometry Enabled Proteomics, Lipidomics and Imaging in Niemann-Pick Type C Disease

Date: Monday, October 17, 2022

Time: 6:15 pm Dinner, 7:15 pm Presentation

Location: Shimadzu Scientific Instrument, Inc. Training Center 7100 Riverwood Drive, Columbia, MD 21046 (Directions)
This will be an in-person meeting. Attendees are required to show a vaccine card (either at the door or in advance using the web form) . If you have submitted your vaccine card before, your status is already recorded.

Dinner: Please RSVP to Andy Qi (andy.yue.qi@gmail.com) by Friday, October 14 if you will be attending the dinner.

Abstract: Mass spectrometry-based proteomics and lipidomics are powerful strategies to understand molecular mechanisms associated with human disease. Our laboratory studies Niemann-Pick Type C (NPC), a fatal, progressive neurodegenerative disorder that arises due to improper trafficking of cholesterol. As a result of the genetic defects in NPC, cholesterol storage is observed in late endosome/lysosome compartments. Subsequently, a series of downstream events occur including neuroinflammation, calcium imbalance, oxidative stress and progressive neuron loss with the disorder being ultimately fatal in the early adulthood years. In an effort to understand pathways associated with the downstream consequences of the genetic cause of NPC, we have employed mass
spectrometry imaging, quantitative proteomics and lipidomics in multiple models of NPC. In this seminar, I will share several examples of integrated ‘omics approach to reveal markers of NPC disease as well as seek insight into cell death in NPC using mass spectrometry.