<p><strong>Join us for a fascinating conversation with Dr. Subhoja Chakraborty from the University of Central Florida, whose cutting-edge research targets the global challenge of malaria drug resistance. Dr. Chakraborty shares her journey from structure-based drug design during her PhD to her recent collaborative work repurposing human kinase inhibitors as rapid, selective antimalarials against drug-resistant Plasmodium falciparum strains.</strong></p><h4><strong>In this episode, you'll learn:</strong></h4><ul><li>How structure-guided approaches reveal potential drug targets, including cysteine proteases like falcipain-2, and kinases implicated in malaria's complex life cycle.</li><li>The power of repurposing kinase inhibitors originally developed for cancer and other diseases, focusing on compound 12, which blocks hemozoin formation and protein kinase 6—key steps in parasite survival.</li><li>Lab techniques such as affinity, gel filtration, and size exclusion chromatography for recombinant protein purification—and how troubleshooting is crucial for high-yield, stable complexes.</li><li>Advances in mass spectrometry for characterizing protein interactions, validating drug targets, and mapping molecular pathways pivotal to malaria therapeutics.</li><li>Tips and lessons for new researchers facing the challenges of sample preparation, complex protocols, and working as part of a collaborative team.</li></ul><p>Dr. Chakraborty’s insights bridge the gap between basic science and translational drug discovery, offering hope for more effective, targeted malaria treatments in a world where resistance to frontline therapies threatens millions.</p><h4><strong>Referenced Papers:</strong></h4><ul><li>"Plasmodium falciparum protein kinase 6 and hemozoin formation are inhibited by a type II human kinase inhibitor exhibiting antimalarial activity" (Cell Chemical Biology, 2025)</li><li>"New insights of falcipain 2 structure from Plasmodium falciparum 3D7 strain" (BBRC, 2022)</li><li>"Structure-Based Optimization of Protease−Inhibitor Interactions to Enhance Specificity of Human Stefin‑A against Falcipain‑2 from the Plasmodium falciparum 3D7 Strain" (Biochemistry, 2023)</li></ul><p>If you’re a student, scientist, or simply passionate about advances in infectious disease research, this episode offers actionable insights, inspiring advice, and a front-row seat to innovation in combating malaria.</p><h3><strong>Video Transcription</strong></h3><h4><strong>From Structural Biology to Drug Discovery: Chromatography and Mass Spectrometry in Malaria Research</strong></h4><h5><strong>Introduction</strong></h5><p>In this discussion, Subhoja shares insights into her research journey, focusing on malaria drug discovery and the role of modern analytical techniques in biological and biomedical research. The conversation is aimed primarily at undergraduate students and early-career researchers interested in chemistry, biotechnology, and life sciences.</p><h5><strong>Research Focus: Malaria Drug Discovery and Kinase Targets</strong></h5><p>Subhoja is currently involved in malaria drug discovery research at the University of Central Florida, where she has been working since beginning her postdoctoral position two years ago. Her earlier PhD research focused on structure-based drug design in malaria, using a combination of in silico approaches, recombinant protein expression, and X-ray crystallography to determine precise three-dimensional structures of target proteins and their inhibitors.</p><p>This structural perspective provided a foundation for her current work, which centers on drug discovery through compound screening and repurposing. A recent publication from her laboratory explores the use of repurposed mammalian CDK-like kinase inhibitors as potential antimalarial agents. While such kinase inhibitors are well known in cancer and cardiovascular research, their application to malaria targets represents a novel and promising approach.</p><p>Kinases are attractive drug targets because of their central role in cell signaling and growth pathways. By targeting specific kinases involved in different stages of the malaria parasite life cycle—whether asexual growth, gametocytogenesis, or differentiation—it may be possible to significantly inhibit parasite growth and progression.</p><h5><strong>Chromatography in Protein Expression and Purification Workflows</strong></h5><p>Chromatography plays a critical role throughout Subhoja’s research. Her experience spans from basic chromatography techniques during her early training to advanced protein purification workflows using affinity chromatography, gel filtration (size exclusion chromatography), and ion exchange chromatography.</p><p>Recombinant proteins are routinely purified using affinity resins such as nickel or cobalt, followed by further purification to remove contaminants. Fast Protein Liquid Chromatography (FPLC) enables compact, stepwise purification workflows suitable for producing proteins for in vitro assays.</p><p>A recurring challenge in this process is the expression of high-molecular-weight proteins, which often accumulate in insoluble fractions or inclusion bodies. Careful selection of expression vectors, host systems, and induction conditions is therefore essential to maximize yield and solubility.</p><h5><strong>Integrating Size Exclusion Chromatography into the Workflow</strong></h5><p>Size exclusion chromatography (SEC) is typically used after affinity purification to further improve protein purity. Following elution with imidazole or glutathione, desalting is required to prevent buffer components from interfering with downstream assays. This is often achieved using desalting columns such as G-25 or PD-10.</p><p>To remove lower-molecular-weight contaminants, finer SEC media—such as Superdex or Sephacryl columns—are employed. Concentration steps using molecular-weight cut-off filters are then applied to obtain the desired protein concentration for functional studies.</p><p>These iterative purification and troubleshooting steps are a routine part of protein biochemistry and reflect the importance of methodical optimization and careful validation.</p><h5><strong>The Role of Mass Spectrometry in Biomolecular Characterization</strong></h5><p>Mass spectrometry is a key analytical tool in Subhoja’s research pipeline, particularly for target identification and validation. In both malaria and cancer research, MS is used alongside chromatography, immunoprecipitation, and pull-down assays to study protein interactions and molecular recognition events.</p><p>Affinity-based mass spectrometry enables the identification of binding partners and interactors, whether studying proteins, long non-coding RNAs, or protein complexes. Techniques such as native MS, tandem affinity purification, and proximity labeling (e.g., TurboID-based workflows) provide deeper insights into molecular networks and signaling pathways.</p><p>These approaches are essential for understanding how candidate drug targets function within complex biological systems.</p><h5><strong>Sample Preparation Challenges in Biological Research</strong></h5><p>Sample preparation remains one of the most challenging aspects of biological experimentation. Whole-cell lysates contain proteases, nucleases, and other components that can rapidly degrade target molecules. Preventing degradation requires minimizing preparation time, maintaining low temperatures, and using appropriate inhibitor cocktails.</p><p>Reproducibility is also critical: biological experiments require multiple replicates, and variability is often unavoidable. Careful handling, protocol optimization, and continuous troubleshooting are essential to ensure reliable results, whether preparing samples for chromatography, mass spectrometry, sequencing, or immunoprecipitation.</p><h5><strong>Advances in Chromatography and MS for Malaria Research</strong></h5><p>Modern advances in chromatography and mass spectrometry significantly enhance malaria research by enabling precise target identification, quantification, and functional characterization. Drug discovery workflows begin with construct design and recombinant expression, followed by purification and interaction studies.</p><p>In malaria research, stage-specific parasite biology requires careful extraction and analysis of proteins from different life cycle stages. Tandem affinity MS, immunoprecipitation, and in vivo validation studies help confirm target relevance and therapeutic potential.</p><p>Recent work on repurposed kinase inhibitors has shown promising results, including inhibition of hemozoin formation—a key detoxification pathway for the malaria parasite—highlighting the potential of such compounds for further development.</p><h5><strong>Malaria, Drug Resistance, and Global Impact</strong></h5><p>Malaria remains a major global health burden, with over 600,000 deaths annually and widespread drug resistance complicating treatment. Artemisinin resistance, particularly associated with mutations in the K13 propeller domain, has driven the search for new targets and therapies.</p><p>During her PhD, Subhoja focused on falcipain-2, a cysteine protease involved in hemoglobin degradation within the parasite. This pathway is critical for parasite survival and has emerged as a promising drug target. Her work revealed that falcipain-2 operates within a larger protein complex responsible for hemoglobin processing and amino acid release.</p><p>Understanding these molecular mechanisms is essential for developing robust, stage-specific antimalarial strategies.</p><h5><strong>Advice for Early-Career Researchers</strong></h5><p>For researchers just starting out, Subhoja emphasizes the importance of hands-on experience. Working directly with cells, lysates, and analytical tools is essential for truly understanding experimental systems. Failure is an inherent part of research, and perseverance is key.</p><p>Motivation, teamwork, careful sample handling, and thorough preparation all contribute to long-term success. Reading extensively, critically evaluating one’s own work, and appreciating incremental progress are vital aspects of a sustainable research career.</p><p>Every successful experiment—no matter how small—represents meaningful progress and contributes to the broader goals of science and medicine.</p><h5><strong>Closing Remarks</strong></h5><p>The discussion highlights how interdisciplinary approaches combining chromatography, mass spectrometry, structural biology, and biochemistry are driving advances in malaria drug discovery. Through careful experimental design, analytical rigor, and collaborative teamwork, researchers can address complex biological challenges and contribute to global health solutions.</p><blockquote><p><strong>This text has been automatically transcribed from a video presentation using AI technology. It may contain inaccuracies and is not guaranteed to be 100% correct.</strong></p></blockquote><blockquote><h4><strong>Concentrating on Chromatography Podcast</strong></h4><p>Dive into the frontiers of chromatography, mass spectrometry, and sample preparation with host David Oliva. Each episode features candid conversations with leading researchers, industry innovators, and passionate scientists who are shaping the future of analytical chemistry. From decoding PFAS detection challenges to exploring the latest in AI-assisted liquid chromatography, this show uncovers practical workflows, sustainability breakthroughs, and the real-world impact of separation science. Whether you’re a chromatographer, lab professional, or researcher you'll discover inspiring content!</p><p>You can find <strong>Concentrating on Chromatography Podcast </strong>in podcast apps:</p><ul><li><a target="_blank" rel="noopener noreferrer" href="https://open.spotify.com/show/1wZg67rCjoGju4yhqxI3tL"><strong>Spotify</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podcasts.apple.com/tz/podcast/concentrating-on-chromatography/id1788429185"><strong>Apple podcast</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podscan.fm/podcasts/concentrating-on-chromatography"><strong>podscan</strong></a></li></ul><p>and on <a target="_blank" rel="noopener noreferrer" href="https://www.youtube.com/@ChromatographyTalk/videos"><strong>YouTube channel</strong></a></p></blockquote>

Affinity, Gel Filtration, Size Exclusion Chromatography: Repurposing Kinase Inhibitors for Malaria

<p><strong>In the week of February 9, the following webinars await you in the field of liquid phase and especially HPLC and LC/MS.</strong></p><blockquote><h4><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinars"><strong>👉 DETAILS AND REGISTRATION IN THE WEBINARS SECTION</strong></a></h4><p><strong>👉 Search and filter in the largest global database</strong> with over <strong>5 000 GC, LC, MS and spectroscopy webinars</strong>.</p></blockquote><h5><strong>1. SelectScience: High-Throughput Stability Screening Strategies for Antibody Formulation</strong></h5><ul><li>Tu, 10.2.2026 17:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5807">Registration</a></li></ul><p>Learn how high-throughput DLS/SLS and rapid-screening DSC accelerate stability assessment of high-concentration antibody formulations, enabling faster, data-driven biologics development.</p><h5><strong>2. Phenomenex: Big Scale, Big Wins – Prep Chromatography Explained</strong></h5><ul><li>We, 11.2.2026 10:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5793">Registration</a></li></ul><p>Learn how to scale analytical methods to preparative HPLC, optimize loading capacity, and understand the limits of preparative columns for pharmaceutical applications.</p><h5><strong>3. ALS Czech Republic: PFAS in Food &amp; Food Contact Material</strong></h5><ul><li>We, 11.2.2026 15:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5816">Registration</a></li></ul><p>Get a practical overview of PFAS in food and food contact materials, including EU and US regulations, key analytical challenges, and reliable PFAS testing strategies.</p><h5><strong>4. New Food Magazine: The Science of Next-Gen Ingredients – Fermentation, Formulation and Function</strong></h5><ul><li>We, 11.2.2026 16:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5720">Registration</a></li></ul><p>Explore how fermentation-driven innovation is transforming functional food ingredients and how advanced analytics optimize flavour, functionality, and stability.</p><h5><strong>5. SCIEX: Accurate Mass Fundamentals – Interpreting and Applying Your Data</strong></h5><ul><li>We, 11.2.2026 19:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5772">Registration</a></li></ul><p>Session 3 focuses on interpreting and applying accurate mass data to confirm compound identity, move beyond basic quantitation, and troubleshoot results for confident reporting.</p><h5><strong>6. Agilent Technologies: Process Analytical Techniques – Online HPLC for Real-Time Monitoring and Control of Bioprocesses</strong></h5><ul><li>Th, 12.2.2026 06:30 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5834">Registration</a></li></ul><p>Discover how PAT HPLC enables near-real-time monitoring of critical quality attributes in bioprocessing, with a case study on charge-variant control by cation-exchange chromatography.</p><h5><strong>7. Thermo Fisher Scientific: Introducing the Orbitrap Excedion Pro Hybrid MS</strong></h5><ul><li>Th, 12.2.2026 11:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5889">Registration</a></li></ul><p>Discover the new Orbitrap Exploris Pro with expanded ETD/EThcD capabilities for confident biopharmaceutical characterization, including intact proteins, PTMs, ADCs, and large biomolecules.</p><h5><strong>8. Waters Corporation: Planning Your NuGenesis Upgrade – Insights and Best Practices for a Smooth Transition</strong></h5><ul><li>Th, 12.2.2026 19:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5833">Registration</a></li></ul><p>Learn how to plan a successful NuGenesis upgrade, transition to Windows 11, and unlock new capabilities such as dashboards for real-time operational insights.</p><h5><strong>9. Thermo Fisher Scientific: Comprehensive Analytical Strategies for Peptide Therapeutics and GLP-1 Agonists with Agilent</strong></h5><ul><li>Th, 12.2.2026 19:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5814">Registration</a></li></ul><p>Explore analytical workflows for peptide therapeutics, including method development, peptide mapping, GLP-1 QC, and LC-MS strategies across Agilent platforms.</p><h5><strong>10. Agilent Technologies: Moving from R&amp;D and Limited QC on a UV-Vis-NIR Instrument to Large-Scale QC Using an Autosampler</strong></h5><ul><li>Th, 12.2.2026 20:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/2104">Registration</a></li></ul><p>This webinar covers practical aspects of adding and using an autosampler to maximize UV-Vis-NIR QC workflows at scale.</p><h5><strong>11. Agilent Technologies: LC Method Transfer – Hidden Challenges &amp; Absolute Solution</strong></h5><ul><li>Fr, 13.2.2026 06:30 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5787">Registration</a></li></ul><p>Discover why LC method transfer between legacy and modern systems is challenging, which hidden parameters affect retention and peak shape, and how to achieve robust, reliable results.</p>

Webinars LabRulezLCMS Week 07/2026

<p><strong>Charge detection mass spectrometry (CDMS) allows direct mass determination of individual ions and is increasingly used to study heterogeneous biological samples. This work demonstrates the use of Orbitrap-based CDMS/Direct Mass Technology (DMT) for quantitative analysis of transthyretin (TTR) tetramer samples below 100 kDa, extending CDMS beyond its traditional qualitative role.</strong></p><p>DMT resolved wild-type and C-terminally modified TTR homotetramers, as well as hybrid tetramers, enabling kinetic analysis of subunit exchange and stability. The approach also quantified thyroxine binding to TTR variants, revealing differences in binding affinity linked to C-terminal modification. By separating overlapping m/z signals through charge measurement, CDMS enables accurate mass and abundance determination, highlighting its potential for quantitative analysis of complex protein systems.</p><blockquote><h4><strong>The original article</strong></h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771"><strong>Dissecting Heterogeneous Populations of Protein-Complex Samples Using Direct Mass Technology</strong></a></h4><p>Robert L. Rider, Jared Hampton, Zhenyu Xi, Carter Lantz, Sangho D. Yun, Weijing Liu, Rosa Viner, Arthur Laganowsky, and David H. Russell*</p><p>Anal. Chem. 2025, 97, 49, 27057–27063</p><p><a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.analchem.5c05771">https://doi.org/10.1021/acs.analchem.5c05771</a></p><h6>licensed under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/"><strong>CC-BY 4.0</strong></a></h6></blockquote><p><strong>Selected sections from the article follow. Formats and hyperlinks were adapted from the original.</strong></p><p>Transthyretin (TTR) is a homotetrameric transport protein that circulates in plasma and cerebrospinal fluid, delivering thyroxine (T<sub>4</sub>) and retinol-binding protein–vitamin A complexes. <a href="javascript:void(0);">(1)</a> The stability of the TTR tetramer is central to its physiological role because dissociation into monomers can initiate misfolding and amyloid formation, leading to systemic or hereditary transthyretin amyloidosis. <a href="javascript:void(0);">(2)</a> Subunit exchange between wild-type (WT) and variant TTR proteoforms, including disease-associated mutations such as V30M and V122I, have been implicated in amyloid progression by generating hybrid tetramers (tetramers containing WT and mutant subunits) with altered stabilities. <a href="javascript:void(0);">(3,4)</a> Ligand binding, particularly at the two thyroxine-binding sites located at the dimer–dimer interface, can kinetically stabilize the tetramer and modulate amyloidogenicity. <a href="javascript:void(0);">(5,6)</a> Accurate measurement of both subunit exchange kinetics and ligand binding stoichiometry is therefore critical for elucidating the TTR dynamics and stability.</p><p>Affinity or sequence tags are widely employed in protein expression, purification, or detection. <a href="javascript:void(0);">(7,8)</a> While these tags are often assumed to be inert, their influence on protein structure and dynamics are rarely examined in detail. <a href="javascript:void(0);">(9,10)</a> Protein tags at the N- and C-terminus of TTR have been shown to have differing gas phase stabilities from those of WT-TTR. <a href="javascript:void(0);">(11)</a> The C-terminus is of particular interest because this region participates in the dimer–dimer interface that governs tetramer stability. <a href="javascript:void(0);">(11,12)</a> Characterizing how the C-terminal tag (CT) (-ASGENLFYQ) affects TTR’s solution stability and ligand binding is not only relevant for understanding TTR dynamics but also provides an example of how expression tags can alter protein dynamics. <a href="javascript:void(0);">(13)</a></p><p>Native mass spectrometry (nMS) has been invaluable for characterizing protein complexes, <a href="javascript:void(0);">(14)</a> yet conventional nMS often struggles with heterogeneous samples where overlapping charge state distributions and adduct heterogeneity limit resolution and quantitation. <a href="javascript:void(0);">(15)</a> Charge detection mass spectrometry (CDMS) addresses these limitations by independently measuring the charge and <i>m</i>/<i>z</i> of individual ions, enabling the direct determination of molecular mass and abundance. Development of CDMS has largely focused on achieving higher mass resolution <a href="javascript:void(0);">(16)</a> and extending measurements toward assemblies into the GDa range. <a href="javascript:void(0);">(17,18)</a> However, there is untapped utility for CDMS experiments other than mass and proteoform determination. Jordan et al. showed the capability to assess conformational heterogeneity of mAb aggregates using the added charge dimension that CDMS provides. <a href="javascript:void(0);">(19)</a> The current work demonstrates that CDMS can separate proteoforms with overlapping <i>m</i>/<i>z</i> values based on charge and quantify their relative abundances in complex mixtures. While nMS is already a highly quantitative technique, our results establish CDMS as an equally powerful tool for quantitative analysis in heterogeneous systems. <a href="javascript:void(0);">(20,21)</a></p><p>Here, we apply Orbitrap-based CDMS/Direct Mass Technology (DMT) using the selective temporal overview of resonant ions (STORI) approach <a href="javascript:void(0);">(22,23)</a> to quantitatively compare WT-TTR and CT-TTR, focusing on two biologically relevant properties: tetramer stability assessed via subunit exchange kinetics and ligand-binding affinity. Conventional nMS cannot fully resolve the overlapping charge states of WT- and CT-TTR or their ligand-bound states. However, DMT can resolve these species by directly measuring the mass (<i>m</i>/<i>z</i> × charge), enabling quantitation of all proteoforms. The data reveal that the CT tag alters tetramer stability and thyroxine-binding affinity, demonstrating the structural sensitivity of TTR to modifications at its C-terminus. More broadly, this work demonstrates the impact that protein tags can have on native protein interactions and highlights the broader utility of quantitative CDMS for probing heterogeneous biological samples.</p><h4><strong>Experimental Section</strong></h4><h5><strong>Data Collection</strong></h5><p>All experiments were conducted on a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/560"><strong>Thermo Scientific Q-Exactive UHMR</strong></a> with added DMT capabilities (Bremen, Germany). Before DMT, mass spectra were collected at various resolving powers (6–200k) for each sample, with the instrument parameters reported in the Supporting Information (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Table S1</a>). For DMT experiments, the trapping gas pressure in the HCD cell was reduced to 0.3–0.8 to attenuate the signal intensity to a single ion level, as well as decreasing the UHV pressure to assist ion retention through the entire transient of Orbitrap analysis. We observed no significant difference between mass spectra collected at various HCD cell pressures (Supporting Information, <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figure S1</a>). For DMT collection, automated ion control (AIC) and 100% target density were used with 200k resolving power.</p><h4><strong>Results and Discussion</strong></h4><p>CDMS has emerged as a powerful tool for analyzing heterogeneous biomolecular samples, enabling accurate, direct mass determination by simultaneously measuring the charge and <i>m</i>/<i>z</i> for individual ions. While CDMS has been widely applied for qualitative analyses, its potential for quantitative and less than MDa applications remains underexplored. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>A shows the theoretical mass spectrum of WT-TTR (14+ to 16+) and CT-TTR (15+ to 17+) homotetramers, where the two proteoforms become increasingly resolved as the charge states increase (&lt;3900 <i>m</i>/<i>z</i>). <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>B zooms in on the 14+ (WT) and 15+ (CT) charge states, highlighting their strong overlap, which prevents accurate deconvolution of the proteoforms by conventional methods. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>C displays theoretical distributions for 0, 1, and 2 T<sub>4</sub> bound states of both WT- and CT-TTR tetramers, where &lt;3900 <i>m</i>/<i>z</i> has observable separation between all proteoforms. However, for the 14+ and 15+ charge states of WT- and CT-TTR, respectively, the 0 T<sub>4</sub>- and 1 T<sub>4</sub>-bound populations overlap (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>D). Furthermore, commonly adducted species (Na<sup>+</sup>, K<sup>+</sup>, and Zn<sup>2+</sup>) observed in experimental spectra broaden these distributions, making it increasingly difficult to distinguish and deconvolute the proteoforms (see <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figure S2</a>). Here, we employ Orbitrap-based CDMS/DMT to overcome this <i>m</i>/<i>z</i> overlap to resolve and quantify hybrid tetramer formation and T<sub>4</sub> binding.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Anal_Chem_2025_97_49_27057_27063_Figure_1_A_Theoretical_mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_47232849d9.jpg" alt="Anal. Chem. 2025, 97, 49, 27057–27063: Figure 1. (A) Theoretical mass spectra of WT-TTR and CT-TTR homotetramers. (B) Zoomed-in view of the 14+ WT-TTR and 15+ CT-TTR distributions to show the large overlap of the proteoforms. (C) Theoretical mass spectra of WT-TTR and CT-TTR homotetramers with thyroxine (T4) binding. (D) Zoomed-in view of the 14+ WT-TTR and 15+ CT-TTR distributions where the 0 and 1 T4 have overlapping distributions. These theoretical distributions do not contain any commonly adducted species (Na+, K+, Zn2+), which broaden the distributions and create more overlap even for the proteoforms in the range 3300–3900 m/z (see Figure S2)." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Anal_Chem_2025_97_49_27057_27063_Figure_1_A_Theoretical_mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_47232849d9.jpg 187w," sizes="100vw" width="1417" height="1182"></p><h5><strong>Thyroxine Binding to TTR Homotetramers</strong></h5><p>Thyroxine is the less active form of a thyroid hormone important for metabolism that binds to TTR for transport throughout plasma and cerebral spinal fluid. <a href="javascript:void(0);">(31)</a> Turnover of T<sub>4</sub> into T<sub>3</sub> (active) occurs after dissociation, where it can then modulate gene expression via binding to nuclear receptors. <a href="javascript:void(0);">(32)</a> The TTR tetramer gains substantial stability as it binds up to 2 T<sub>4</sub> at the tetramer interface, decreasing tetramer dissociation and SUE. <a href="javascript:void(0);">(33)</a> This has been shown previously to decrease the amyloidogenic rate of TTR, which led to tafamidis (similar in structure to T<sub>4</sub>) to be designed and is currently the only drug that is approved for clinical treatment of TTR amyloidosis. <a href="javascript:void(0);">(34)</a> Measuring the difference in binding affinity between TTR proteoforms may provide insight into regions of TTR or TTR intermolecular/intramolecular interactions that are important for binding of small molecules such as tafamidis and T<sub>4</sub>.</p><p>DMT was further applied to quantify T<sub>4</sub> binding to WT- and CT-TTR homotetramers, highlighting the technique’s utility in probing protein–ligand interactions. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig3">Figure 3</a>A shows a representative mass spectrum of TTR homotetramers in the presence of T<sub>4</sub>. While ligand-bound species can be observed, homotetramers cannot be confidently resolved across the entire 3000–5000 <i>m</i>/<i>z</i> range. By leveraging the charge-resolving capabilities of DMT, we achieve separation of the homotetramers (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig3">Figure 3</a>B,C) and the 0, 1, and 2 ligand-bound states. The 2D plot clearly shows the gain in resolution achieved when charge is simultaneously measured with <i>m</i>/<i>z</i> by separating the 14+ and 15+ charge states for WT and CT, respectively, in the range 3900–4200 <i>m</i>/<i>z</i>. Additionally, using ion mobility does not provide the same kind of 2D resolution due to the similarity in arrival times for the homotetramer proteoforms, as evidenced by <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figures S4 and S5</a> (see the Supporting Information). These data provide evidence that when ion mobility is able to separate out species that overlap in <i>m</i>/<i>z</i> yet differ in mobility, CDMS could be an alternative or used complementarily since the species likely also differ in charge.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Anal_Chem_2025_97_49_27057_27063_Figure_3_A_Mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_with_thyroxine_binding_61b1e98a94.jpg" alt="Anal. Chem. 2025, 97, 49, 27057–27063: Figure 3. (A) Mass spectra of WT-TTR and CT-TTR homotetramers with thyroxine binding. Ligand binding can be resolved, but homotetramers cannot be confidently identified. Charge states labeled are for WT; CT is always one charge state higher at the same m/z range. (B) DMT heatmap resolving WT-TTR and CT-TTR homotetramers with the additional measurement of charge. (C) Deconvoluted mass spectrum from DMT analysis. Both homotetramers and their ligand binding are resolved, and fit for analysis is shown in red. (D) Mole fraction of each homotetramer and their thyroxine binding species. Error bars represent the standard deviation of replicates (n = 3). The significance for each ligand state is in respect to the left adjacent state. *p &lt; 0.05." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Anal_Chem_2025_97_49_27057_27063_Figure_3_A_Mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_with_thyroxine_binding_61b1e98a94.jpg 181w," sizes="100vw" width="1266" height="1094"></p><h4><strong>Conclusion</strong></h4><p>This work demonstrates that quantitatively, Orbitrap-based CDMS/DMT can determine differences in protein-complex stability and ligand binding. By directly comparing WT- with CT-TTR, we show that the CT tag accelerates tetramer dissociation while enhancing T<sub>4</sub> binding affinity. These results indicate that the C-terminus, located at the dimer–dimer interface, plays a more significant role in TTR stability and ligand recognition than previously appreciated. <a href="javascript:void(0);">(12)</a> Even the addition of a short peptide sequence perturbs noncovalent interactions at the interface, likely altering solvent accessibility, and the dynamics of the thyroxine binding channel. <a href="javascript:void(0);">(37,54)</a> Such findings underscore the importance of evaluating how seemingly minor sequence modifications, such as affinity tags, can influence fundamental biophysical properties.</p><p>Beyond TTR, this work positions quantitative CDMS as a broadly applicable strategy for analyzing heterogeneous protein systems, where charge domain separation overcomes the resolution limits of <i>m</i>/<i>z</i> domain measurements in traditional nMS experiments. While much of the field has emphasized extending CDMS to ultrahigh masses and maximal resolution, <a href="javascript:void(0);">(16,18)</a> our results highlight the underexplored potential of applying the method in the 1000–10,000 <i>m</i>/<i>z</i> range common to nMS experiments. This capability is directly relevant to heterogeneous membrane protein complexes, which often display broad distributions of oligomeric states, PTMs, lipid, and ligand adducts that complicate spectra. <a href="javascript:void(0);">(48,55)</a> Similarly, mAbs can oligomerize and exhibit mass heterogeneity from variable glycosylation, affecting pharmacokinetics, effector function, and stability. <a href="javascript:void(0);">(19)</a> CDMS may resolve and quantify such proteoforms in a single experiment without the need for charge reduction or chemical derivatization. <a href="javascript:void(0);">(48,56,57)</a></p>

Dissecting Heterogeneous Populations of Protein-Complex Samples Using Direct Mass Technology

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<h4><strong>European Free Educational Webinar Series</strong></h4>
<p><strong>Let&#39;s go back to the basics of Chromatography, Mass Spectrometry, Data Analysis and Trouble-shooting: understanding the importance of the basics will enable you to be more effective in your daily laboratory life.</strong></p>
<h4><strong>EPISODE 7</strong></h4>
<p><strong>Introduction to Mass Spectrometry</strong></p>
<p><strong>What will you learn?</strong></p>
<ul>
<li>Fundamentals of MS: LC/MS, LC/MS/MS &amp; TOF Systems</li>
<li>How to modify your LC Method when adding MS Detection</li>
</ul>
<blockquote>
<p><strong>Prezenter:</strong>  Antonia Wierzbicki (Principal MS Market Dev Manager, EMEA, Waters Corporation)</p>
</blockquote>
<blockquote>
<p>Antonia Wierzbicki is a MS market development manager at Waters working in EMEA. Antonia has BSc in Pharmaceutical Science and a MSc in Cancer Pharmacology.</p>
</blockquote>
<blockquote>
<p>Following several years working as an analytical chemist in drug development roles within both academic labs and contract research organizations, Antonia has more recently spent time working with analytical chemists to provide solutions using cutting edge technologies to meet their needs and requirements, with a specific interest in ultra-sensitive quantitation of small molecules.</p>
</blockquote>
<blockquote>
<p>Antonia is based in Cambridge UK and keen to connectwith like-minded scientists in the field.</p>
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<h4><strong>What&#39;s next?</strong></h4>
<p>Full Webinar Series Episodes List is available <a href="https://event.on24.com/wcc/r/4551012/F69479929A905500D8B21508527807E5/5385652"><strong>here</strong></a></p>
<p>Back to Basics - Sample Preparation: Theory and Overview</p>
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<li>Tuesday, May 07, 2024, 11:00 AM CEST</li>
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<li>Wednesday, June 05, 2024, 11:00 AM CEST</li>
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<p>Back to Basics - Basics of Liquid Chromatography</p>
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<li>Wednesday, October 02, 2024, 11:00 AM CEST</li>
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Waters Corporation: Back to Bacisc Free Educational Webinar Serries

Introduction to Mass Spectrometry

Fundamentals of MS in LC/MS, LC/MS/MS & TOF Systems.

<ul>
<li><p><strong>Discuss what GC-MS/MS is and what applicaitons it is used for (Dioxins, POPs, etc.)</strong></p>
</li>
<li><p><strong>Transition into an overview of APGC as a solution</strong></p>
</li>
<li><p><strong>Discuss challenges or limitations of the current GC/MS/MS technology</strong></p>
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<p>Webinar Learning Objectives:</p>
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<li><p>Understanding GC-MS/MS and Its Applications:- Discuss the principles of gas chromatography-mass spectrometry (GC-MS/MS) and its role in analytical chemistry.- Explore specific applications of GC-MS/MS, including its use in detecting dioxins, persistent organic pollutants (POPs), and other environmental contaminants.</p>
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<li><p>Introduction to APGC (Atmospheric Pressure Gas Chromatography):-. Provide an overview of Atmospheric Pressure Gas Chromatography (APGC) as an alternative solution to traditional GC-MS/MS.- Highlight the advantages and unique features of APGC, such as improved sensitivity, reduced matrix effects, and enhanced selectivity.</p>
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<li><p>Challenges and Innovations in GC-MS/MS Technology:- Identify the current challenges and limitations faced by GC-MS/MS technology.- Discuss recent innovations and advancements aimed at overcoming these challenges.- Emphasize the importance of using nitrogen as a carrier gas for GC-MS/MS analysis, considering its inertness, availability, and compatibility with various detectors.</p>
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</ul>
<blockquote>
<p><strong>Prtesenter:</strong> Frank Dorman (Senior Principal Market Development Mgr, Waters Corporation)</p>
</blockquote>
<blockquote>
<p>Frank Dorman is currently Senior Principal Market Development Manager for Waters focusing on their global environmental business and, concurrently, a Resident Scholar in the Chemistry Department at Dartmouth College in Hanover, NH where he is active in teaching analytical chemistry to undergraduates and graduate students.</p>
</blockquote>
<blockquote>
<p>In his role at Waters, Frank manages the research-focused environmental market, external collaborations, and interfaces with R&amp;D for new product development. Prior to this, Frank was an Associate Professor in the Department of Biochemistry and Molecular Biology (BMB) sat Penn State University in University Park, PA. At Penn State, Frank served as a member of the Graduate Faculty in: Biochemistry, Microbiology and Molecular Biology (BMMB), Chemistry (CHEM), Biogeochemistry (BGC) and the Forensic Science Program (FRNSC) and the Center for Molecular Toxicology and Carcinogenesis. Franks scientific interests are in gas and liquid chromatography and fundamental characterization, instrumentation and column development, as well as mass spectrometry and atomic spectroscopy as applied to trace analysis in complex sample matrices.</p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Sarah Dowd (Principal Mass Spectrometry Applications Specialist, Waters Corporation)</p>
</blockquote>
<blockquote>
<p>Sarah Dowd joined Waters as a mass spectrometry application specialist in 2015 after earning her PhD in analytical chemistry from the University of Illinois at Urbana Champaign.</p>
</blockquote>
<blockquote>
<p>In her eight years at Waters in the Americas application lab, Sarah has collaborated with many customers looking to expand the MS capabilities of their laboratories with Water&#39;s instruments and software. Specializing in analyses in food, environmental, and polymeric materials characterization, she has done extensive work looking at environmental contaminants with tandem quadrupole and high resolution mass spectrometers.</p>
</blockquote>
<blockquote>
<p>One of the hot topics for the past couple of years is the analysis of per- and polyfluoroalkyl substances (PFAS) and Sarah has collaborated with customers and other scientists within Waters to guide the next phase of PFAS testing with Waters mass spectrometry systems.</p>
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Waters Corporation: APGC Roundtable: Unveiling the Pathways of GC-MS/MS Evolution

APGC Roundtable: Unveiling the Pathways of GC-MS/MS Evolution

Discuss what GC-MS/MS is and what applicaitons it is used for (Dioxins, POPs, etc.)

APGC Roundtable: Unveiling the Pathways of GC-MS/MS Evo

<p><strong>Join us for an insightful webinar where we will explore the critical aspects of differentiating good from bad data and how this distinction can significantly influence your results. From screening to quantification, discover the value of targeted data analysis workflows using non-targeted data with our innovative software and hardware.</strong></p><p>Find by Formula algorithm. Learn to identify the most suitable MS/MS approach for your experiments, initiate quantitation for your compounds of interest, and incorporate retention times (RTs) and MS/MS spectra into a custom database and library.</p><p>This session is designed to enhance your understanding and application of Q-TOF data analysis, ensuring robust and reliable outcomes.</p><blockquote><p><strong>Presenter:</strong> Hannah Florance (Agilent Technologies)</p><p>Hannah has had multiple roles in the life sciences, starting as a protein chemist, before moving into proteomics and then metabolomics. A major part of her time working in academia involved running LC and GCMS core facilities supporting projects ranging from synthetic biology to cancer research. She is currently an LCMS applications specialist for Agilent.<br><br><strong>Presenter:</strong> Stefan Schaebler (Application Specialist LC/MS, Agilent Technologies)</p><p>Stefan completed his PhD in Biology, specializing in LC-MS-based lipidomics and metabolomics. Following his doctoral studies, he joined Agilent Technologies as an LC/MS Application Specialist. In this role, Stefan focuses on small molecule applications using LC-QTOF, with a strong emphasis on software tools and data interpretation.</p></blockquote>

Agilent Technologies: MassHunter Masterclass Months

MassHunter Qual – The Solid Pillar in Q-TOF Data Analysis

We will explore the critical aspects of differentiating good from bad data and how this distinction can significantly influence your results.

<p><strong>Join our upcoming webinar on the MassHunter Quant Screener Tool to discover how to harness the power of quantitative analysis for effective screening and identification of potential suspect compounds.</strong></p><p>This session will provide in-depth guidance on creating methods from PCDL databases, evaluating result parameters, and generating straightforward summary reports. Additionally, learn how retention time (RT) prediction can enhance your screening process by significantly accelerating and simplifying large database searches.</p><p>Don’t miss this opportunity to elevate your analytical capabilities!</p><blockquote><p><strong>Presenter:</strong> &nbsp;Jonathan Spencer (Application Specialist, Agilent Technologies)</p><p>Jonathan studied BSc Natural Sciences at the University of Nottingham and later went on to Sheffield Hallam University to study a MSc in Forensic Science.</p><p>Following graduation, he spent 2 years as a Confirmatory Analyst in an anti-doping and forensic toxicology lab, before joining Agilent as an LC/MS Applications Scientist. At Agilent, he focuses on small molecule applications using LC/TQ and LC/Q-TOF in fields of like food, forensic and environmental analysis.</p></blockquote>

MassHunter Quant Screener Tool

Discover how to harness the power of quantitative analysis for effective screening and identification of potential suspect compounds. 

<p style="margin-bottom:6.0pt;" id="isPasted"><span name="summary"><strong fr-original-style="">In this presentation, we will explore groundbreaking advancements in the bioanalysis of antisense oligonucleotides (ASO), achieving remarkable sub ng/mL limits of quantitation (LOQ). We’ll dive into practical and scalable solutions that ensure precise quantitation of these complex molecules.</strong></span></p><p><span name="summary">Discover innovative sample preparation techniques designed to maximize recovery, enhance repeatability, and boost LC-MS sensitivity. Additionally, we’ll showcase the latest LC-MS hardware from Waters, which not only delivers industry-leading negative ionization efficiency, but also saves valuable bench space and reduces utility usage compared to competitors.</span></p><h5><span name="summary"><strong>Key Learning Objectives:&nbsp;</strong></span></h5><ul><li><span name="summary" data-teams="true" id="isPasted" dir="ltr"><strong fr-original-style="">Explore scalable solutions for quantifying complex oligonucleotides across a wide range of concentrations.</strong></span></li><li><span name="summary" data-teams="true" id="isPasted" dir="ltr"><strong fr-original-style="">Discover practical approaches that enhance recovery, repeatability, and LC‑MS sensitivity.</strong></span></li><li><span name="summary" data-teams="true" id="isPasted" dir="ltr"><strong fr-original-style="">Take advantage of the opportunity to attend the presentation live, where you'll have the chance to ask questions, engage, clarify, and deepen your understanding of the latest innovations in bioanalysis.</strong></span></li></ul><div><blockquote><p><strong>Presenter:</strong> Andrew Leightner (<span>Senior Principal Market Development Manager, Pharmaceuticals and Biopharmaceuticals, Waters Corporation)</span></p><div><p align="LEFT"><span>Andy Leightner has over 10 years of experience serving the pharma market from contract research organizations. He specialized in method development and validation leveraging LC, GC, and mass spectrometry to meet complex client needs. He supports pharmaceutical and biopharmaceutical discovery and development in the Americas for Waters Corporation. Andy received a bachelors degree in biology from the University of Wisconsin-Madison.</span></p></div></blockquote></div>

Elevating Oligonucleotide Bioanalysis: LOQ, Dynamic Range, and Innovative Sample Preparation Techniques

We will explore groundbreaking advancements in the bioanalysis of antisense oligonucleotides (ASO), achieving remarkable sub ng/mL limits of quantitation (LOQ).

Oligonucleotide Bioanalysis: LOQ, Dynamic Range, SamplePrep

<div><div><div><p><strong>Alithea Biotechnology was founded in 2019 by Fanny Giannou and Tim Fugmann to support Biopharma globally on the development of innovative therapies targeting HLA-presented peptides. Alithea has a significant track record in the absolute quantification of HLA peptides, off-target toxicity predictions and target discovery.</strong></p><p>In addition, HLA-Compass is Alithea's cloud-accessible HLA peptide database featuring the measurement of a total of 1.4 Million HLA peptides in 4160 healthy tissue, tumor tissue and cancer cell line samples for target validation and off-target toxicity prediction.</p><h5><strong>Why to join this webinar:</strong></h5><ul><li><strong>The timsTOF Ultra can lead to high quality immunopeptidomes from limited sample</strong></li><li><strong>Extensive HLA databases can significantly speed up the T-Cell-Receptor therapy development process</strong></li><li><strong>The time is ripe to bring immunopeptidomics into clinical routine</strong></li></ul><blockquote><p><strong>Presenter:</strong> Tim Fugmann, Ph.D. (Chief Scientific Officer and Co-Founder, Alithea Biotechnology GmbH, Berlin, Germany)</p><p>Tim Fugmann got his Ph.D. from ETH Zurich, on mass-spectrometric discovery of antibody targets and disease biomarkers. Later, he was leading the target discovery efforts at Philochem, before moving to the Max-Delbrueck-Centrum for Molecular Medicine in Berlin. He was later appointed professor for MS-based proteomics at JLU Giessen. In 2019 he co-founded Alithea Bio UG, which is focusing on immunopeptidomics, a topic which Tim Fugmann studied since 2012.</p></blockquote></div></div></div>

Bruker: Unlocking the full potential of immunopeptidomics with the timsTOF Ultra

Unlocking the full potential of immunopeptidomics with the timsTOF Ultra

Alithea has a significant track record in the absolute quantification of HLA peptides, off-target toxicity predictions and target discovery.

The potential of immunopeptidomics with the timsTOF Ultra

<p><strong>Hear about the latest advancements in translational proteomics and metabolomics. From the molecular mechanisms of disease pathology to the latest technological developments in diagnostics and treatment.</strong></p><h5><strong>Key Learning Objectives:</strong></h5><ul><li>Spatial proteomics to assess health and diseases</li><li>Absolute quantitation of human proteins</li><li>The latest innovations in proteomics and metabolomics instrumentation and data analysis</li><li>Biomarker-guided precision medicine</li></ul><h4><strong>Day 1 – October 30</strong></h4><h5><strong>15:00 – 15:50 GMT: The Human Protein Atlas – Creating a Pan-Disease Resource Based on Next Generation Blood Profiling</strong></h5><ul><li>Mathias Uhlén, PhD (KTH Royal Institute of Technology)</li></ul><h5><strong>15:50 – 15:55 GMT:</strong> Networking Break</h5><h5><strong>15:55 – 16:15GMT: Mitigating Sorter-Induced Cellular Stress with Cartridge, Microfuildics-Based Sorting</strong></h5><ul><li>Crystal Montoya (Miltenyi Biotec)</li></ul><h5><strong>16:15 – 16:20 GMT:</strong> Networking Break</h5><h5><strong>16:20 – 16:40 GMT: Speaker to be announced</strong></h5><h5><strong>16:40 – 16:45 GMT</strong>: Networking Break</h5><h5><strong>16:45 – 17:35 GMT: Spatial Tissue Proteomics to Assess Health and Disease</strong></h5><ul><li>Fabian Coscia, PhD (Max Delbrück Center)</li></ul><h5><strong>17:35 – 17:40 GMT:</strong> Networking Break</h5><h5><strong>17:40 – 18:00 GMT: The Sulpho-Phospho-Vanillin Assay: Accurate Lipid Normalization in Quantitative Lipidomics</strong></h5><ul><li>Karri Basso, PhD (University of Florida)</li></ul><h5><strong>18:00 – 18:05 GMT:</strong> Networking Break</h5><h5><strong>18:05 – 18:55 GMT: Proteomics for Cancer Precision Medicine</strong></h5><ul><li>Janne Lehtiö, PhD (Karolinska Instutet)</li></ul><h5><strong>18:55 – 19:00 GMT: </strong>Networking Break</h5><h5><strong>19:00 – 19:20 GMT: How Breakthroughs in Depth, Scale and Speed are Unlocking New Proteomic Discovery</strong></h5><ul><li>Aaron Gajadhar, PhD (Seer Bio)</li></ul><h5><strong>19:20 – 19:25 GMT: </strong>Networking Break</h5><h5><strong>19:25 – 19:55 GMT:</strong> Phantom Metabolites: Unraveling Metabolic Shadows</h5><ul><li>Gary Siuzdak, PhD (Scripps Research Institute)</li></ul><h5><strong>19:55 GMT:</strong> End of Day 1</h5><div><div><div><h5><strong>Who Should Attend:</strong></h5><ul><li>Scientists and researchers seeking to expand their knowledge</li><li>Pharmaceutical and biotech professionals driving drug development</li><li>Clinicians looking to improve patient care</li><li>Academicians exploring new research avenues</li><li>Graduate students and postdoctoral fellows building their careers</li></ul><blockquote><p><strong>Presenter: </strong>Mathias Uhlén, PhD (Professor, KTH - Royal Institute of Technology)</p><p><strong>Presenter:&nbsp;</strong>Christoph Borchers, PhD (Professor, McGill University)</p><p><strong>Presenter:</strong>&nbsp;Janne Lehtiö, PhD (Professor, Karolinska Institutet)</p><p><strong>Presenter:</strong>&nbsp;Crystal Montoya (Senior Marketing Product Manager, Miltenyi Biotec)</p><p><strong>Presenter:</strong>&nbsp;Kari Basso, PhD (Director of Mass Spectrometry Research and Education, University of Florida)</p><p><strong>Presenter:&nbsp;</strong>Fabian Coscia, PhD (Group Leader, Max Delbrück Center)</p><p><strong>Presenter:</strong>&nbsp;Simone Sidoli, PhD (Assistant Professor, Albert Einstein College of Medicine)</p><p><strong>Presenter:</strong>&nbsp;Hagen Magnus Gegner, PhD (Content and Digital Marketing, CTC Analytics)</p><p><strong>Presenter:</strong>&nbsp;Matt Willetts, PhD (Proteomics Applications Manager, Bruker Daltonics)</p><p><strong>Presenter:&nbsp;</strong>Matteo Tardelli, PhD (Senior Biomarker Scientist, Owlstone Medical)</p><p><strong>Presenter:&nbsp;</strong>Aaron Gajadhar, PhD (Director, Strategic Applications, Seer)</p><p><strong>Presenter:&nbsp;</strong>Gary Siuzdak, PhD (Professor and Senior Director, Scripps Research Institute)</p></blockquote></div></div></div>

Technology Networks: Advances in Proteomics & Metabolomics 2024

Advances in Proteomics & Metabolomics 2024 (Day 1)

Hear about the latest advancements in translational proteomics and metabolomics. 

Advances in Proteomics & Metabolomics 2024  (Day 1)

<p><strong>Hear about the latest advancements in translational proteomics and metabolomics. From the molecular mechanisms of disease pathology to the latest technological developments in diagnostics and treatment.</strong></p><h5><strong>Key Learning Objectives:</strong></h5><ul><li>Spatial proteomics to assess health and diseases</li><li>Absolute quantitation of human proteins</li><li>The latest innovations in proteomics and metabolomics instrumentation and data analysis</li><li>Biomarker-guided precision medicine</li></ul><h4><strong>Day 2 – October 31</strong></h4><h5><strong>15:00 – 15:50 GMT: A Novel Strategy for the Absolute Quantification of Human Proteins</strong></h5><ul><li>Christoph Borchers, PhD (McGill University)</li></ul><h5><strong>15:50 – 15:55 GMT: </strong>Networking Break</h5><h5><strong>15:55 – 16:15 GMT: From Single Cells to the Metaproteome: Latest Developments in timsTOF Technology for Proteomics</strong></h5><ul><li>Matt Willetts, PhD (Bruker)</li></ul><h5><strong>16:15 – 16:20 GMT: </strong>Networking Break</h5><h5><strong>16:20 – 17:10 GMT: Single-Cell Chromatin Proteomics to Investigate the Biology of Exceptional Longevity</strong></h5><ul><li>Simone Sidoli, PhD (Albert Einstein College of Medicine)</li></ul><h5><strong>17:10 – 17:15 GMT: </strong>Networking Break</h5><h5><strong>17:15 – 17:35 GMT: Optimizing Metabolomics Workflows: From Sample Preparation to Multi-omics Integration</strong></h5><ul><li>Hagen Magnus Gegner, PhD (CTC Analytics)</li></ul><h5><strong>17:35 – 17:40 GMT:</strong> Networking Break</h5><h5><strong>17:40 – 18:10 GMT: Analyzing Metabolic Responses to a Standardized Meal Challenge Using Exhaled Breath</strong></h5><ul><li>Matteo Tardelli, PhD (Owlstone Medical)</li></ul><h5><strong>18:10 GMT: </strong>Event Close</h5><h5><strong>Who Should Attend:</strong></h5><ul><li>Scientists and researchers seeking to expand their knowledge</li><li>Pharmaceutical and biotech professionals driving drug development</li><li>Clinicians looking to improve patient care</li><li>Academicians exploring new research avenues</li><li>Graduate students and postdoctoral fellows building their careers</li></ul><blockquote><p><strong>Presenter: </strong>Mathias Uhlén, PhD (Professor, KTH - Royal Institute of Technology)</p><p><strong>Presenter:&nbsp;</strong>Christoph Borchers, PhD (Professor, McGill University)</p><p><strong>Presenter:</strong>&nbsp;Janne Lehtiö, PhD (Professor, Karolinska Institutet)</p><p><strong>Presenter:</strong>&nbsp;Crystal Montoya (Senior Marketing Product Manager, Miltenyi Biotec)</p><p><strong>Presenter:</strong>&nbsp;Kari Basso, PhD (Director of Mass Spectrometry Research and Education, University of Florida)</p><p><strong>Presenter:&nbsp;</strong>Fabian Coscia, PhD (Group Leader, Max Delbrück Center)</p><p><strong>Presenter:</strong>&nbsp;Simone Sidoli, PhD (Assistant Professor, Albert Einstein College of Medicine)</p><p><strong>Presenter:</strong>&nbsp;Hagen Magnus Gegner, PhD (Content and Digital Marketing, CTC Analytics)</p><p><strong>Presenter:</strong>&nbsp;Matt Willetts, PhD (Proteomics Applications Manager, Bruker Daltonics)</p><p><strong>Presenter:&nbsp;</strong>Matteo Tardelli, PhD (Senior Biomarker Scientist, Owlstone Medical)</p><p><strong>Presenter:&nbsp;</strong>Aaron Gajadhar, PhD (Director, Strategic Applications, Seer)</p><p><strong>Presenter:&nbsp;</strong>Gary Siuzdak, PhD (Professor and Senior Director, Scripps Research Institute)</p></blockquote>

Advances in Proteomics & Metabolomics 2024 (Day 2)

<div><div><div><p><strong>Pure MHC, a pioneer in immunopeptidomics, has partnered with Bruker, a leader in state-of-the-art mass spectrometry, to demonstrate one of Pure MHC’s immunopeptidomics workflows. In this Live from the Lab webinar, tissue sample processing, data acquisition with a Bruker timsTOF Ultra, and data analysis will be reviewed as tools for the development and validation of HLA peptide targets for immunopeptidomic development.</strong></p><p><strong>Key Learning Objectives:</strong></p><ul><li>Get insights into Pure MHC's sample preparation strategies to maximize the yield of immunopeptides from tissue samples</li><li>Discover how the unparalleled sensitivity and robustness of the Bruker timsTOF Ultra empowers users to maximize the potential of their immunopeptide samples</li><li>Understand data processing workflows for both DDA and DIA data processing</li></ul><blockquote><p><strong>Presenter:</strong> Curtis McMurtrey, Ph.D. (Director of Immunoproteomics, Pure MHC, LLC, Oklahoma City, OK, USA)</p><p>Dr. McMurtrey earned his Ph.D. in Microbiology and Immunology from the University of Oklahoma Health Sciences Center in 2010. He currently serves as the Director of Immuno-Proteomics at Pure MHC, LLC.</p><p>Dr. McMurtrey has studied HLA and its role in immunity since 2005. He is a member of American Society for Histocompatibility and Immunogenetics (ASHI) and holds the distinction of having won four ASHI Top Scholar Awards, more than any other scientist in the history of ASHI. Dr. McMurtrey is most notable for his work on West Nile virus epitope discovery and validation with HLA-A*02:01 and B*07:02; epitopes he discovered have been successfully tested in a WNV vaccine (collaboration with Drs. Hansen and Diamond at Washington University). His most recent accolades come from discovery of MR1 ligands from Mycobacterium tuberculosis (Mtb) as well as over 200 novel ligands from Toxoplasma gondii utilizing Deep Ligand Sequencing (DLS).</p><p>Dr. McMurtrey has expertise in BSL-3 containment techniques, protein purification, HLA ligand isolation, HPLC separation, mass spectrometric analysis, ELISPOT, and multicolor flow cytometry as well as provides bioinformatics expertise. To date, he has directed mass spectrometry (both IDA and SWATH) acquisition as well as comparative analysis and interpretation for a wide variety of MHC ligands including those from tuberculosis, toxoplasmosis, influenza, WNV, HIV and multiple cancers. Dr. Curtis McMurtrey oversees DLS acquisition and analyses and also manages database library collection.</p><p><strong>Presenter: </strong>Jason R. Krawic, Ph.D. (Business Development Manager, Pure MHC, LLC, Oklahoma City, OK, USA)</p><p>Dr. Krawic earned his Master’s degree in Biomolecular Sciences from Central Connecticut State University in 2012 before returning to academia and earning his Ph.D. in Microbiology and Immunology from the University of Oklahoma Health Sciences Center in 2024. He currently serves as the Director of Business Development at Pure MHC, LLC.</p><p>Dr. Krawic began his scientific career teaching Microbiology, Biology, and Chemistry to community college students in Connecticut and Oklahoma. He has studied HLA and non-classical MHC molecules since 2018. He is most recognized for discovering multiple isomeric conformations of MR1 ligands, as well as his work in MHC Class I and Class II ligands and cancer immunotherapies.</p><p>Dr. Krawic’s expertise ranges from classical microbiology and bacteriology to HPLC separation, protein purification, negative ion mode small molecule mass spectrometry, DDA, DIA and MRM acquisition and a variety of bioinformatics tools. In addition to his scientific career, Dr. Krawic has more than a decade of experience in sales and retail management. With this skill set he combines his science and sales backgrounds to serve Pure MHC’s customer base.</p><p><strong>Presenter: </strong>Kris Looney, MBA (President, Pure MHC, LLC, Austin, TX, USA)</p><p>As President of Emergent Technologies, the manager of Pure MHC, Kris Looney is responsible for conceiving and executing key business initiatives, developing strategic plans, and managing business processes including accounting, marketing, intellectual property, and business development. Kris has more than two decades of experience as a business generalist with a background in start-ups, management, accounting, marketing, negotiation, and sales.</p><p>Before joining Emergent, Kris served as the COO and Interim CEO of the American Red Cross of Central Texas, where he balanced multiple stakeholder needs with service responsibilities in a competitive philanthropic environment. Prior to that, he was the CFO of Transformation Enzyme Corporation, where his financial management and business development helped a bootstrapped entrepreneurial start-up become a leader in the nutritional supplement market. Kris has a B.A. in marketing and an M.B.A. from the University of Texas at Austin.</p><p><strong>Presenter: </strong>Matt Willetts, Ph.D. (Proteomics Applications Manager, Bruker Scientific LLC, Billerica, MA, USA)</p><p>Matt received his Ph.D. in mass spectrometry with Prof. Malcolm Clench at Sheffield Hallam University in the UK. He then joined Waters as the Technical Marketing Specialist for LCMS and MALDI products, focusing on application development for proteomics-based workflows. Matt joined Bruker in 2010 and is responsible for proteomics applications and support in North America.</p></blockquote><p>&nbsp;</p></div></div></div>

Bruker: Pure MHC's immunopeptidomics workflow with the timsTOF Ultra

Pure MHC's immunopeptidomics workflow with the timsTOF Ultra

Tissue sample processing, data acquisition with a Bruker timsTOF Ultra, and data analysis for immunopeptidomic development.

<p><strong>This presentation discusses the work being done to understand how drugs work and how they can be repurposed for new indications. Prof. Küster’s lab uses various technologies and methods, such as sample preparation, mass spectrometry, and informatics, to study the proteome and fosso-proteome of cancer patients.</strong></p><p>The goal is to find the right drug for the right person by understanding what is going wrong in the patient and what the drugs can do. By studying drug-protein interactions and pathway engagement in a dose-dependent fashion, this research aims to make better treatment recommendations. The lab has developed a technology platform that allows for the systematic profiling of kinase inhibitors and the measurement of proteome expression changes in response to drugs.</p><p>This information can help prioritize biological effects and facilitate drug repurposing. This presentation highlights the importance of studying proteins in understanding drug mechanisms of action and identifying potential targets for cancer treatment.</p><p><strong>Learning points:</strong></p><ul><li>Importance of Repurposing Drugs &nbsp;</li><li>Role of Proteomics in Precision Oncology &nbsp;</li><li>Dose-Dependent Analysis &nbsp;</li></ul><blockquote><p><strong>Presenter: </strong>Prof. Bernhard Küster (Technical University Munich)</p><p>Bernhard Küster holds a chemistry degree from Cologne, a PhD in Biochemistry from Oxford and did a PostDoc at the EMBL in Heidelberg and the University of Southern Denmark. After seven years as Vice President Analytical Sciences and Informatics at Cellzome (now GSK), he became.​</p><p>Full Professor of Proteomics at the TU Munich in 2007. He also directs the Bavarian Biomolecular Mass Spec-trometry Center and the Clinical Mass Spectrometry Center Munich.​</p><p>Bernhard’s research focuses on proteomics and its application to chemical and cancer biology. He is interested in understanding how cancer drugs actually work and has received an ERC Advanced Grant in 2019 aiming to integrate proteomics into precision medicine. Bernhard has received several awards, including from HUPO for a draft human proteome and his contri-butions to chemical proteomics. Bernhard is a member of the German National Academy of Science, Leopoldina and has co-founded two start-up companies that operate in the area of proteomics and artificial intelligence.</p></blockquote>

Thermo Fisher Scientific: Understanding drugs using proteomics

Understanding drugs using proteomics

This presentation highlights the importance of studying proteins to understand drug mechanisms and identify potential targets for cancer treatment

LCMS webinars focusing on LC/MS/MS - page 30