Speaker: Robert Cole, Johns Hopkins University School of Medicine

Topic: What’s on your albumin?

Date: Monday, March 20, 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, March 17 if you will be attending the dinner.

Abstract: Environmental exposures contribute to chronic disease risk substantially more than heritable genetic variants. Outdoor air pollution is a complex environmental
mixture which is responsible for over 4 million deaths each year, an impact that is projected to rise over the next several decades. The International Agency for Research on Cancer (IARC) has declared outdoor air pollution to be Group 1 human carcinogen. Outdoor air is a complex mixture of volatile organic toxins and carcinogens (e.g., aldehydes and benzene), sulfur dioxide, nitrogen oxides, polycyclic aromatic hydrocarbons, and particulate matter. Assessing personal exposure to environmental toxicants in complex mixtures, such as outdoor air pollution, is a critical challenge for predicting disease risk. Thus, developing and validating biomarkers which reveal exposure to these complex mixtures would advance individual risk analysis. Using human serum albumin (HSA)-based biomonitoring, we reported dosimetric relationships between adducts at HSA Cys34 and ambient air pollutant levels. However, modifications at other sites in HSA may reveal a great number of novel adducts and provide a panel of exposure biomarkers for disease risk. To bridge this gap, we developed a novel untargeted mass spectrometry-based method, termed Pan-Protein Adductomics (PPA),
to agnostically detect and quantify modifications at multiple residues in human serum albumin (HSA). Our PPA method combines nanoflow-liquid chromatography, gas-phase fractionation, overlapping-window data-independent acquisition, and high-resolution tandem mass spectrometry to assay modifications on HSA. Our initial application of PPA is to assess temporal changes in HSA modifications in non-smoking women exposed to high levels of outdoor air pollution. While we are currently focused on modifications in albumin, the PPA approach is applicable to any protein and may expand the knowledge base of protein modifications.

Thank you to our 2022-2023 sponsors!

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.