Speaker: Mazdak Taghioskoui, Trace Matters Scientific
Topic: Overcoming Fundamental Limits in Mass Spectrometry: SPion®, Super Mass Spectrometry, and the Delayed-ESI Technique
Date: Monday, December 15, 2025
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, December 12 if you will be attending the dinner.
Abstract: Despite decades of progress, modern mass spectrometry has advanced primarily through incremental refinements built on fundamentally unchanged architectures, and while these improvements have expanded capabilities, the underlying instrumentation has not kept pace with the increasing analytical demands of proteomics, biomedicine, in-situ chemical analysis, and other rapidly evolving fields. This persistent mismatch highlights the need for disruptive technologies that reconceptualize how ions are generated, transferred, and measured. Over the past several years, I have been developing such technologies, and in this seminar I will present three complementary innovations designed to directly address these long-standing limitations. I will first introduce SPion®, a NASA award–winning flexible ion-guide architecture that enables near-lossless ion transfer over extended distances and decouples the ion source from the instrument, thereby supporting handheld probes, robotic imaging platforms, and dendritic mass spectrometry, in which multiple instruments acquire data from a single ionization event. I will then discuss the conceptual and practical foundations of Super Mass Spectrometry, a distributed, cluster-based measurement framework that independently scales sensitivity and scan speed, mitigates the bandwidth mismatch between LC and MS, and provides a feasible path toward high-dynamic-range mass spectrometry. Within this broader framework, I will also highlight the Delayed-ESI technique, which creates compositionally identical but temporally staggered ion beams to enable deterministic re-measurement, extend dynamic range, and improve repeatability and quantitative fidelity in LCMS workflows. Collectively, these advances establish a new class of scalable mass-spectrometry architectures engineered to overcome severe ion losses, restricted intrinsic dynamic range, and raster-limited sampling—fundamental constraints that prevent conventional instruments from producing high-fidelity digital representations of complex biological samples—and together they outline a path toward the next generation of mass-spectrometry technologies aligned with the scientific and industrial challenges of the coming decades.
Lightning Talks
Integrative Blood Proteomics Reveals the HuBP Atlas of over 10,000 Proteins Informing Human Physiology and Disease
Zhenyu Sun, Ph.D.
Johns Hopkins University School of Medicine
Blood is a rich source of clinical information, yet no resource systematically maps protein detectability across sample types, workflows, and disease states. We developed the Human Blood Proteome (HuBP) database, integrating protein abundance, detectability, and reproducibility across plasma workflows and whole-blood disease cohorts. Using DIA with complementary enrichment strategies, we identified 9,965 proteins in healthy plasma and profiled PDAC, ccRCC, and LUAD whole blood, detecting 8,002–8,009 proteins and 498 disease-specific markers. In total, HuBP compiles 10,463 nonredundant proteins, providing a quantitative atlas that supports experimental optimization, biomarker discovery, and precision medicine applications.
Painting the Proteome: SPOTTER for High-Plex Spatial Protein Maps
Yuanwei (Bay) Xu, Ph.D.
Johns Hopkins University School of Medicine
Spatial proteomics aims to identify and quantify proteins and PTMs in situ with regional resolution, linking molecular states to tissue architecture and microenvironments. Dissecting molecular heterogeneity at relevant spatial scales is critical for understanding the biological and pathological roles of functional proteins. Current technologies include antibody-based imaging, which typically tracks a limited panel of markers, and LMD-based LC–MS workflows, which isolate and analyze a small number of regions separately. In contrast, SPOTTER directly labels tissue proteins with chemical tags across the entire section, generating arrays of ~100–200 µm microregions. A single SPOTTER experiment could report proteome-wide abundance distributions across all spots, enabling scalable, high-plex spatial maps using standard instruments and workflows.
