October 2019 Meeting

Speaker: Leslie Hicks, University of North Carolina at Chapel Hill

Topic: Investigating plant-derived antimicrobial peptides using PepSAVI-MS

Date: Monday, October 21st, 2019

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

Location: Shimadzu Scientific Instruments, Inc. Training Center 7100 Riverwood Drive, Columbia, MD 21046 (Directions)

Dinner: Please RSVP to Meghan Burke (meghan.burke@nist.gov) by Friday, October 18th if you will be attending the dinner.

Abstract: As current methods for antibiotic drug discovery are being outpaced by the rise of antimicrobial resistance, new methods and innovative technologies are crucial to replenish our dwindling arsenal of antimicrobial therapeutics. While natural products are a well-studied source of biologically active small molecules, peptidyl factors contributing to their medicinal properties remain largely unexplored. To this end, we have developed the PepSAVI-MS to identify bioactive peptide targets from complex biological samples. The developed platform is highly versatile as it is adaptable to any natural product source of peptides and can test against diverse physiological targets, including bacteria, fungi, and cancer cells for which there is a developed bioassay. As such, we demonstrated extension of this pipeline to fungal and bacterially-sourced AMPs and are beginning to probe the vast array of botanical natural product sources to prioritize highly active species for downstream analysis.

September 2019 Meeting

Speaker: Joseph Zaia, Boston University School of Medicine

Topic: Proteomics, glycomics, and glycoproteomics of matrisome molecules

Date: Monday, September 16th, 2019

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

Location: Shimadzu Scientific Instruments, Inc. Training Center 7100 Riverwood Drive, Columbia, MD 21046 (Directions)

Dinner: Please RSVP to Meghan Burke (meghan.burke@nist.gov) by Friday, September 16th if you will be attending the dinner.

Abstract: The most straightforward applications of proteomics database searching involve intracellular proteins. While intracellular gene products number in the thousands, their well-defined post-translational modifications (PTMs) makes database searching practical. By contrast, cell surface and extracellular matrisome proteins pass through the secretory pathway where many become glycosylated, modulating their physicochemical properties, adhesive interactions, and diversifying their functions. While matrisome proteins number only a few hundred, their high degree of complex glycosylation multiplies the number of theoretical proteoforms by orders of magnitude. Given that extracellular networks that mediate cell-cell and cell-pathogen interactions in physiology depend on glycosylation, it is important to characterize the proteomes, glycomes and glycoproteomes of matrisome molecules that exist in a given biological context. In this presentation, I will summarize proteomics approaches for characterizing matrisome molecules, with an emphasis on applications to brain diseases.

Fall 2019-Spring 2020 Meeting Schedule

The schedule for Fall 2019-Spring 2020 is here!

Sept. 16, 2019 – Joseph Zaia (Boston University), Vendor Show featuring WBMSDG sponsors
Oct. 21, 2019 – Leslie Hicks (UNC-Chapel Hill, ASMS Travel Award)
Nov. 18, 2019 – Will Brinckerhoff (NASA)
Dec. 16, 2019 – Asher Newsome (Smithsonian Institution)
Jan. 13, 2020 – Allison Scott (University of Maryland-Baltimore)
Feb. 10, 2020 – Joe Cannon (Merck)
Mar. 16, 2020 – Carlos Larriba-Andaluz (Purdue, ASMS Travel Award)
Apr. 20, 2020 – Ben Neely (NIST)
May 18, 2020 – Ira Lurie (George Washington University)
June 15, 2020 – Post-ASMS Poster Night, Travel Award Presentations


Speaker: Liangliang Sun, Michigan State University

Topic: Top-down Proteomics Using Capillary Zone Electrophoresis-Tandem Mass Spectrometry

Date: Monday, March 11, 2019

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

Location: Hampton Inn & Suites Columbia, 7045 Minstrel Way, Columbia, MD 21046 (Directions)

Dinner: Please RSVP to Yan Wang (yanwang@umd.edu) by Friday, March 8th if you will be attending the dinner.

Abstract: Genome-level and transcriptome-level information cannot accurately reflect proteome-level information because post-transcriptional regulations modulate gene expression,because protein post-translational modifications (PTMs) influence protein function, and because most proteins in cells function as complexes with proteins, RNAs, metals or other small molecules. Characterization of the proteome is imperative to understand the roles played by proteins, protein PTMs and even protein complexes in development and diseases.

Top-down proteomics is a well-known strategy for large-scale characterization of proteome at the intact protein level and is very useful for high-resolution characterization of proteoforms that represent all kinds of protein molecules derived from the same gene due to gene-level variations, RNA-level alternative splicing, and protein-level PTMs. The number of proteoforms in the human proteome has been estimated to be over 1 million. High-capacity separation of proteoforms before electrospray ionization-mass spectrometry and tandem mass spectrometry (ESI-MS and MS/MS) is essential for deep and high-resolution top-down proteomics.

The top-down proteomics community has made tremendous efforts in improving liquid chromatography (LC)-MS and MS/MS for top-down proteomics. We argue that capillary zone electrophoresis (CZE)-MS and MS/MS is another powerful tool for top-down proteomics because CZE can approach high-capacity separation of intact proteins and because CZE-MS has shown obviously higher sensitivity than LC-MS for protein detection. In my talk, I will talk about our recent work on boosting CZE-MS and MS/MS for large-scale and highly sensitive top-down proteomics. I will also introduce our work on developing CZE-MS and MS/MS methodologies for native top-down proteomics that aims to characterize the endogenous protein complexes in cells in discovery mode.

February 2019 Meeting (note location change)

Speaker: W. Andy Tao, Purdue University

Topic: Analyses of Protein Phosphorylation and Their Applications in Liquid Biopsy

Date: Monday, February 11, 2019

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

Location: University of Maryland College Park, room 1208, Biology-Psychology building, 4066 Campus Drive, College Park, MD 20742 (parking: 200 Regents Dr, College Park, MD 20742) (Directions)

Dinner: Please RSVP to Yan Wang (yanwang@umd.edu) by Friday, February 8th if you will be attending dinner.

Abstract: Protein kinases and their substrates comprise extensive signaling networks that regulate many diverse cellular functions. However, methods and techniques to systematically identify kinases directly responsible for specific phosphorylation events have remained elusive. Here we describe integrated proteomic strategies to dissect kinase networks in high throughput and demonstrate their applications in multiple systems. Our group has introduced a set of chemical tools and proteomics strategies to analyze protein phosphorylation, in particular, to identify direct kinase substrates and upstream kinases. Recently, for the first time, we identified thousands of phosphoproteins isolated from small volumes of plasma samples and quantitatively measured phosphoproteins that are significantly higher in patients diagnosed with breast cancer as compared to healthy controls. Our studies demonstrate that the development of phosphoproteins as disease biomarkers is highly feasible and may transform disease early detection and monitoring.