Speaker: Lisa Jenkins, National Cancer Institute

Topic: Investigation into the Mechanism and Targets of an Antiviral Zinc Finger Inhibitor

Date: Monday, May 11, 2026

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

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

Dinner: Please RSVP to Sheng Feng (SFeng@som.umaryland.edu) by Friday, May 9 if you will be attending the dinner.

Abstract: Covalent modification of target proteins is a well-established mechanism of action for small molecule inhibitors. Cysteine residues in particular have been exploited for their reactivity toward electrophilic molecules. SAMT-247 is a mercaptobenzamide thioester that covalently acetylates cysteines in the zinc-coordinating domains of the HIV nucleocapsid (NC) protein. We have used mass spectrometry to investigate the mechanism of viral inactivation of NC by SAMT-247, identifying multiple sites of covalent modification that resulted from SAMT reaction. This SAMT-247-promoted reaction leads to loss of zinc binding by the protein, with concomitant loss of protein structure and function. Although it has low cytotoxicity in animal models, recent studies have indicated that it affects other protein targets in uninfected cells, for example leading to increased immune cell functions. We have used global proteomics approaches have been used to better understand other protein targets of SAMT-247 in THP-1 cells. Although minimal effects are observed when unstimulated THP-1 monocyte cells were treated with SAMT-247, many potential targets were identified when the THP-1 cells were stimulated with phorbol 12-myristate 13-acetate/Ionomycin (PMA/Iono) before SAMT-247 treatment. Among the affected proteins, several with zinc-coordinating domains and/or reactive cysteine residues were found. Further study of reaction of SAMT-247 with two potential targets verified that they are modified by the inhibitor. The increased effects of SAMT-247 in stimulated immune cells suggests that this molecule could be developed to target diseases other than HIV.

Lightning Talk
Automatic Blood Protein Enrichment by Magnetic-COF Polymers
Yuanyu Huang, Johns Hopkins University

Abstract: Blood proteome is a highly informative biological fluid, reflecting physiological and pathological states across the entire body. Automated Magnetic-COF workflow achieves deep, reproducible, and scalable blood proteome profiling across plasma, serum, and whole blood, with reduced dominance of high-abundance proteins and improved access to low-abundance species. The platform maintained low variability and broad physicochemical coverage without introducing major enrichment bias, which enabled identification of more than 4000 blood proteins with the throughput of 30 samples per day. Applied to a 110-sample PDAC serum cohort, it delivered stable cohort-scale performance, identified clinically relevant differential proteins, and highlighted biomarker candidates such as APOE and CEACAM5 with promising diagnostic value. Collectively, these findings establish Magnetic-COF–based automation as a robust strategy for high-throughput blood proteomics and translational biomarker discovery in PDAC.

Speaker: Christopher A. LeClair, National Center for Advancing Translational Sciences (NCATS), NIH

Topic: How Many Samples!?: Automation Facilitates High-Throughput Sample Preparation for Analytical Analysis

Date: Monday, April 13, 2026

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

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

Dinner: Please RSVP to Sheng Feng (SFeng@som.umaryland.edu) by Friday, April 10 if you will be attending the dinner.

Abstract: The endeavor of increasing experimental capacity to reduce the therapeutic discovery and development timeline has heavily focused on throughput and cycle time. Most advancements center on improvements to instrument sensitivity, sampling time, sample size, data processing speed, and data quality, enabling thousands of samples to be analyzed down to a seconds per sample time scale while generating large, information-rich datasets. However, sample preparation remains a bottleneck as methods and protocols tend to be manual, time-consuming, and often disconnected from research workflows. The Analytical Chemistry Core (ACC) within the Division of Preclinical Innovation (DPI) at NCATS has leveraged automation technologies to develop innovative platforms for higher throughput in sample purification, processing, and preparation. This initiative has resulted in chromatography and mass spectrometry standardized workflows and processes that not only increase experimental capacity but reduce operational inefficiencies. To provide effective purification support in an efficient and expedient manner, the ACC developed a centralized liquid chromatography sample purification and processing platform for the rapid progression of crude reaction mixtures to purified compounds. This platform facilitates the addition of thousands of compounds annually to the NCATS compound library. Furthermore, we successfully developed an automated, high-throughput 384-well plate format sample preparation platform for the reproducible extraction of proteins from cells for MS-based proteomics. The platform is highly adaptable, being applied to the isolation and analysis of other substrates of interest (i.e., lipids, metabolites), as well as using other biological source materials such as human-derived (i.e., serum) and whole organism (i.e., C. elegans). The continued development and optimization of automated platforms will allow us to readily accommodate the handling, preparation, and analysis for large numbers of varied samples, providing greater analytical support to research programs.

Lightning Talk
Enhancing Spatial Biology with Atmospheric and Vacuum MALDI Platforms
Francine Yanchik-Slade, Ph.D.
Shimadzu Scientific Instruments

Abstract: Mass spectrometry imaging (MSI) has emerged as a powerful analytical technique for visualizing the spatial distribution of biomolecules within complex samples, offering critical insights for spatial omics, drug distribution studies, and molecular diagnostics. Shimadzu provides a comprehensive, fully integrated MALDI-based imaging workflow that supports every stage of the process, from matrix application through data acquisition and advanced data analysis. To accommodate diverse experimental needs, Shimadzu offers both atmospheric-pressure and vacuum MALDI platforms. The iMScope QT combines high-resolution atmospheric-pressure MALDI with a built-in optical microscope, enabling precise co-registration and ensuring accurate targeting of regions of interest. Complementing this, the MALDI-80X0 delivers robust, high-throughput MALDI imaging performance in a compact benchtop format suited for any laboratory environment. This presentation will highlight real-world applications of these systems that are advancing spatial omics and driving innovation through streamlined imaging workflows.

Speaker: Elizabeth Neumann, University of California, Davis

Topic: Spatial Multiomics towards Understanding Neurological diseases

Date: Monday, March 9, 2026

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

Location: University of Maryland College Park, Chemistry (Directions)

Dinner: Please RSVP to Sheng Feng (SFeng@som.umaryland.edu) by Friday, March 6 if you will be attending the dinner.

Abstract: Organ systems are composed of unique cell types that actively coordinate to enable higher order functions. Even slight deviances in the molecular or cellular states of these systems can result in debilitating disorders whose severity, treatment course, and overall treatment outcome vary widely from patient to patient. This level of complexity likely contributes to promising therapeutics failing within clinical trials and, thus, require further exploration. Thus, the Neumann lab focuses on developing and applying multimodal imaging and profiling techniques to study complex human diseases, such as renal cell carcinoma, Alzheimer’s Disease, and spina bifida. Beyond disease, we also develop methods for spatially assessing exogenous agents, including pharmaceuticals, toxins, and plastics, within organ and whole animal models.

Lightning Talk
Stellar MS: Redefining targeted proteomics with a quadrupole, collision cell and linear ion trap architecture
Romain Huguet, Ph.D.
Nominal Mass Product Management team, Thermo Fisher Scientific

Targeted mass spectrometry is traditionally applied at the final stage of the biomarker discovery pipeline for the quantification of limited numbers of candidate analytes. While targeted MS delivers superior quantitative accuracy, precision, and specificity, its broader application in upstream discovery and verification studies has been constrained by limited multiplexing capacity and throughput. The new Stellar MS platform integrates a quadrupole mass filter, collision cell, and radial ejection linear ion trap architecture that expands the practical range of targeted proteomics. Hardware and instrument control advancements, combined with a real-time Adaptive Retention Time (RT) algorithm that compensates for chromatographic shifts, enable substantially narrower acquisition windows. This approach supports the targeting of 5,000–8,000 peptides per hour, enabling robust high-plex quantitative workflows.
For low-plex applications, this platform further enhances specificity and sensitivity through an MS³ acquisition strategy, reducing interference and increasing quantitative confidence for small, high-value peptide panels.
By unifying high-multiplex throughput and low-plex analytical rigor within a single system, this platform extends the utility of targeted MS across discovery, verification/ validation, and translational proteomics applications