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.<h4>In this episode, you'll learn:</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>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.<h4>Referenced Papers:</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>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.<h3>Video Transcription</h3><h4>From Structural Biology to Drug Discovery: Chromatography and Mass Spectrometry in Malaria Research</h4><h5>Introduction</h5>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.<h5>Research Focus: Malaria Drug Discovery and Kinase Targets</h5>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.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.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.<h5>Chromatography in Protein Expression and Purification Workflows</h5>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.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.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.<h5>Integrating Size Exclusion Chromatography into the Workflow</h5>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.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.These iterative purification and troubleshooting steps are a routine part of protein biochemistry and reflect the importance of methodical optimization and careful validation.<h5>The Role of Mass Spectrometry in Biomolecular Characterization</h5>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.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.These approaches are essential for understanding how candidate drug targets function within complex biological systems.<h5>Sample Preparation Challenges in Biological Research</h5>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.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.<h5>Advances in Chromatography and MS for Malaria Research</h5>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.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.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.<h5>Malaria, Drug Resistance, and Global Impact</h5>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.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.Understanding these molecular mechanisms is essential for developing robust, stage-specific antimalarial strategies.<h5>Advice for Early-Career Researchers</h5>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.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.Every successful experiment—no matter how small—represents meaningful progress and contributes to the broader goals of science and medicine.<h5>Closing Remarks</h5>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.<blockquote>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.</blockquote><blockquote><h4>Concentrating on Chromatography Podcast</h4>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!You can find Concentrating on Chromatography Podcast in podcast apps:<ul><li><a target="_blank" rel="noopener noreferrer" href="https://open.spotify.com/show/1wZg67rCjoGju4yhqxI3tL">Spotify</a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podcasts.apple.com/tz/podcast/concentrating-on-chromatography/id1788429185">Apple podcast</a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podscan.fm/podcasts/concentrating-on-chromatography">podscan</a></li></ul>and on <a target="_blank" rel="noopener noreferrer" href="https://www.youtube.com/@ChromatographyTalk/videos">YouTube channel</a></blockquote>

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

In the week of February 9, the following webinars await you in the field of liquid phase and especially HPLC and LC/MS.<blockquote><h4><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinars">👉 DETAILS AND REGISTRATION IN THE WEBINARS SECTION</a></h4>👉 Search and filter in the largest global database with over 5 000 GC, LC, MS and spectroscopy webinars.</blockquote><h5>1. SelectScience: High-Throughput Stability Screening Strategies for Antibody Formulation</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>Learn how high-throughput DLS/SLS and rapid-screening DSC accelerate stability assessment of high-concentration antibody formulations, enabling faster, data-driven biologics development.<h5>2. Phenomenex: Big Scale, Big Wins – Prep Chromatography Explained</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>Learn how to scale analytical methods to preparative HPLC, optimize loading capacity, and understand the limits of preparative columns for pharmaceutical applications.<h5>3. ALS Czech Republic: PFAS in Food &amp; Food Contact Material</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>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.<h5>4. New Food Magazine: The Science of Next-Gen Ingredients – Fermentation, Formulation and Function</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>Explore how fermentation-driven innovation is transforming functional food ingredients and how advanced analytics optimize flavour, functionality, and stability.<h5>5. SCIEX: Accurate Mass Fundamentals – Interpreting and Applying Your Data</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>Session 3 focuses on interpreting and applying accurate mass data to confirm compound identity, move beyond basic quantitation, and troubleshoot results for confident reporting.<h5>6. Agilent Technologies: Process Analytical Techniques – Online HPLC for Real-Time Monitoring and Control of Bioprocesses</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>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.<h5>7. Thermo Fisher Scientific: Introducing the Orbitrap Excedion Pro Hybrid MS</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>Discover the new Orbitrap Exploris Pro with expanded ETD/EThcD capabilities for confident biopharmaceutical characterization, including intact proteins, PTMs, ADCs, and large biomolecules.<h5>8. Waters Corporation: Planning Your NuGenesis Upgrade – Insights and Best Practices for a Smooth Transition</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>Learn how to plan a successful NuGenesis upgrade, transition to Windows 11, and unlock new capabilities such as dashboards for real-time operational insights.<h5>9. Thermo Fisher Scientific: Comprehensive Analytical Strategies for Peptide Therapeutics and GLP-1 Agonists with Agilent</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>Explore analytical workflows for peptide therapeutics, including method development, peptide mapping, GLP-1 QC, and LC-MS strategies across Agilent platforms.<h5>10. Agilent Technologies: Moving from R&amp;D and Limited QC on a UV-Vis-NIR Instrument to Large-Scale QC Using an Autosampler</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>This webinar covers practical aspects of adding and using an autosampler to maximize UV-Vis-NIR QC workflows at scale.<h5>11. Agilent Technologies: LC Method Transfer – Hidden Challenges &amp; Absolute Solution</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>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.

Webinars LabRulezLCMS Week 07/2026

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.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.<blockquote><h4>The original article</h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771">Dissecting Heterogeneous Populations of Protein-Complex Samples Using Direct Mass Technology</a></h4>Robert L. Rider, Jared Hampton, Zhenyu Xi, Carter Lantz, Sangho D. Yun, Weijing Liu, Rosa Viner, Arthur Laganowsky, and David H. Russell*Anal. Chem. 2025, 97, 49, 27057–27063<a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.analchem.5c05771">https://doi.org/10.1021/acs.analchem.5c05771</a><h6>licensed under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/">CC-BY 4.0</a></h6></blockquote>Selected sections from the article follow. Formats and hyperlinks were adapted from the original.Transthyretin (TTR) is a homotetrameric transport protein that circulates in plasma and cerebrospinal fluid, delivering thyroxine (T4) 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.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>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 m/z 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 m/z 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>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 (m/z × 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.<h4>Experimental Section</h4><h5>Data Collection</h5>All experiments were conducted on a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/560">Thermo Scientific Q-Exactive UHMR</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.<h4>Results and Discussion</h4>CDMS has emerged as a powerful tool for analyzing heterogeneous biomolecular samples, enabling accurate, direct mass determination by simultaneously measuring the charge and m/z 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 m/z). <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 T4 bound states of both WT- and CT-TTR tetramers, where &lt;3900 m/z has observable separation between all proteoforms. However, for the 14+ and 15+ charge states of WT- and CT-TTR, respectively, the 0 T4- and 1 T4-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+, K+, and Zn2+) 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 m/z overlap to resolve and quantify hybrid tetramer formation and T4 binding.<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"><h5>Thyroxine Binding to TTR Homotetramers</h5>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 T4 into T3 (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 T4 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 T4) 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 T4.DMT was further applied to quantify T4 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 T4. While ligand-bound species can be observed, homotetramers cannot be confidently resolved across the entire 3000–5000 m/z 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 m/z by separating the 14+ and 15+ charge states for WT and CT, respectively, in the range 3900–4200 m/z. 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 m/z yet differ in mobility, CDMS could be an alternative or used complementarily since the species likely also differ in charge.<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"><h4>Conclusion</h4>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 T4 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.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 m/z 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 m/z 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>

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

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Everything from the world of analytical chemistry in one place. We connect people in solving their problems. At Labrulez you will find all the necessary information easily, quickly and clearly. Stop searching and start finding.

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Organomation, founded in 1959, designs and manufactures high-quality nitrogen evaporators and extraction systems. Known for innovation and durability, their lab instruments are used globally for efficient sample preparation with strong customer support.

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Agilent Technologies

Bruker

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SelectScience

Evosep Biosystems

Join this webinar to learn how to simplify, speed-up, and standardize your proteomics sample preparation for LC-MS.
The PreOmics team will introduce the PreOmics easy-to-use iST technology. This fast 3-step workflow is designed to be a great support for both those new to proteomics and experts alike. The all-in-one iST kits are compatible with a variety of starting materials, including mammalian and plant samples, different types of tissue and cells, as well as various biological fluids in label-free and chemical labelling applications.The protocols promise an incredibly fast processing time (&lt;2.5 hours) and are easily applicable without compromising sample quality or proteomic depth. Furthermore, iST can be fully automated to further increase standardization, reproducibility, and throughput.
The speakers will also introduce PreON, a fully automated sample preparation platform, as well as different levels of automation for established liquid handling platforms. The varying applications for the iST technology ranging from global proteomics to pre-clinical studies will also be discussed.
<h5>Key learning objectives</h5>
<ul>
<li>Discover best practices for proteomics sample preparation with solutions for new users and proteomics experts alike</li>
<li>Learn more about fast, easy, and reliable sample preparation protocols for LC-MS-based proteomics</li>
<li>Explore automation, standardization, and upscaling of proteomics sample preparation</li>
<li>Learn more about the applications of iST sample preparation kits and solutions in global proteomics as well as pre-clinical research</li>
</ul>
<h5>Who should attend?</h5>
<ul>
<li>Users working with proteomics sample preparation for LC-MS:</li>
<li>Researchers, scientists, principal investigators, group leaders and department heads, lab assistants from biotech/pharma industry, CROs, university hospitals as well as academia</li>
<li>Biomedical and clinical scientists in translational and pre-clinical research</li>
<li>Application scientists and technical support</li>
<li>Distributors of sample preparation systems for LC-MS</li>
<li>Scientists looking for a straightforward approach to start with proteomics</li>
</ul>
<blockquote>
Presenter: Dr. Ingrid Albrecht-Walz (PreOmics GmbH)
</blockquote>
<blockquote>
Dr. Ingrid Albrecht-Walz joined PreOmics in 2022 as Product Manager for Kits &amp; Reagents. She received her Ph.D. in Biology from the University of Munich, Germany, working on the interaction of different viruses. For the past 10 years, Dr. Albrecht-Walz has worked in the field of in vitro diagnostics of infectious diseases. Since proteomics is a highly promising tool for preclinical and diagnostic applications, Dr. Albrecht-Walz decided in 2022 to follow this opportunity at PreOmics.
</blockquote>
<blockquote>
Presenter: Dr. Vincenzo Romaniello (PreOmics GmbH)
</blockquote>
<blockquote>
Dr. Vincenzo Romaniello joined PreOmics in 2021 as Product Manager for Automation Systems. He received his Ph.D. in molecular physiology from the University of Göttingen, Germany. During the past 5 years, Dr. Romaniello has worked in both technical and application support roles for automated sample preparation workflows with major biotech and human diagnostics scientific suppliers. As a result, he has experience in PreOmics automation solutions, and Tecan and Eppendorf systems.
</blockquote>
<blockquote>
Presenter: Dr. Zuzana Demianova (PreOmics GmbH)
</blockquote>
<blockquote>
Dr. Demianova joined PreOmics in 2021 as a Market Development Manager BioPharma and scientific advisor. Assessing proceedings and challenges in the pharma and biopharma field Dr. Demianova introduces PreOmics’ solutions in customer workflows to enable scientific discovery. She thereby partakes also in the development and market introduction of new products as well as optimization and application of established solutions. Prior to PreOmics, Dr. Demianova was application support specialist at Sciex, concentrating on customer support and training. Later on, she was promoted to a global leader in proteomics, which finally led up to her new role as a biopharma application scientist with a focus on “-omics” and biopharma applications using CE and LC-MS technologies.
</blockquote>
<blockquote>
Presenter: Blake Forman (SelectScience)
</blockquote>
<blockquote>
Blake studied chemistry at the University of Surrey, UK, and further went on to study a master’s in chemistry at the University of Southampton, UK. Blake has previously worked in the Medicines and Healthcare Products Regulatory Agency (MHRA) lab at LGC and as a technical sales specialist for Waters. As a member of the Editorial team, he now plays an integral role in shaping the content on SelectScience.
</blockquote>

SelectScience: Next generation solutions for proteomics sample preparation

Next generation solutions for proteomics sample preparation

Join this webinar to learn how to simplify, speed-up, and standardize your proteomics sample preparation for LC-MS.

A novel spatial technique, DISCO-MS, combines whole-organ/whole-organism clearing and imaging, deep-learning-based image analysis, robotic tissue extraction, and ultra-high-sensitivity mass spectrometry with the Bruker timsTOF instrument family. This combination enables DISCO-MS to perform unbiased proteome analysis of preclinical and clinical tissues from quantity-limited materials after unbiased imaging of entire specimens in 3D.
In this webinar, you will learn about a new experimental approach that combines whole tissue clearing, dia-PASEF®, and trapped ion mobility spectrometry (TIMS) mass spectrometry to analyze the spatial proteome of complex tissue structures. The webinar will detail how with this technique, researchers were able to:
<ul>
<li>Analyze the proteome of preclinical and clinical tissues after identification of regions of interest using 3D imaging, followed by robotic tissue extraction</li>
<li>Achieve early unbiased detection and characterization of subtle tissue perturbations across pathologies</li>
<li>Benefit from the use of ultra-high sensitivity and robust timsTOF mass spectrometers</li>
</ul>
<h5>Key learning objectives</h5>
<ul>
<li>Discover the new experimental approach that combines whole tissue clearing, dia-PASEF®, and TIMS mass spectrometers can be used to analyze the spatial proteome of complex tissue structures</li>
<li>Understand how researchers were able to analyze the proteome of specific tissue regions following 3D imaging to enable robotic tissue extraction</li>
<li>Learn about the unparalleled sensitivity and robustness the timsTOF platform offers with 4D-Proteomics™ which enables researchers to delve deeper into proteome analysis and gain greater insights</li>
</ul>
<blockquote>
Presenter: Dr. Harsharan Singh Bhatia (Institute for Tissue Engineering and Regenerative Medicine (iTERM))
</blockquote>
<blockquote>
Dr. Harsharan Singh Bhatia is the Omics technologies team leader at the Institute for Tissue Engineering and Regenerative Medicine (iTERM), Helmholtz Munich. He completed his Ph.D. at the University of Freiburg, Germany, studying the neuroprotective role of dietary antioxidants. Bhatia worked as a postdoctoral researcher at UCLA, where he investigated the impact of dietary manipulations on rodent behavior. He later returned to the University of Freiburg to work as a research associate at the University Clinic, exploring epigenetic factors&#39; regulation of microglial function. In 2017, Bhatia joined iTERM to study chronic neuroinflammation using DISCO tissue clearing and spatial-omics tools.
</blockquote>
<blockquote>
Presenter: Jemima Arnold (Editorial Team, SelectScience)
</blockquote>
<blockquote>
Jemima studied Cellular and Molecular Medicine at the University of Bristol, UK, and as a member of the Editorial team, she now plays an integral role in shaping the content on SelectScience.
</blockquote>

SelectScience: Spatial proteomics in three-dimensional intact specimens

Spatial proteomics in three-dimensional intact specimens

A new experimental approach that combines whole tissue clearing, dia-PASEF®, and TIMS MS to analyze the spatial proteome of complex tissue structures.

Webinar in collaboration with the Polish Society of Metabolomics.
<h3>14:00 - 14:20 Benefits of Trapped Ion Mobility Spectrometry (TIMS) for Metabolomics and Lipidomics</h3>
<ul>
<li>Presenter: Dr. Stefanie Wernisch ( Business Development Manager Metabolomics/Multiomics, Bruker Daltonics Bremen, Germany)</li>
</ul>
After revolutionizing the area of proteomics, trapped ion mobility spectrometry (TIMS) is now conquering the fields of metabolomics and lipidomics. Bruker&#39;s unique timsTOF technology addresses the complexity of biological samples by adding an orthogonal dimension of separation before mass spectrometric analysis, thus reducing the complexity of MS/MS data and improving annotation confidence for untargeted analysis. The ability to determine Collisional Cross Sections (CCS) can further aid identification and outlier detection in lipidomics studies.
<h3>14:20 - 14:40 SpatialOMx® for in-depth 4D-Lipidomics™</h3>
<ul>
<li>Presenter: Dr. Janina Oetjen (Application Specialist MALDI Imaging, Bruker Daltonics Bremen, Germany)</li>
</ul>
The combined possibilities of ESI and MALDI in one instrument enables powerful SpatialOMx® applications. In short, ion mobility-based annotation can connect confident LC-TIMS-MS/MS identification with meaningful spatial information from MALDI Imaging, specifically in the field of lipidomics. Further, segmentation results based on lipid imaging can define specific regions of interest for subsequent, in-depth analysis. Thus, the information content of MALDI Imaging can be enhanced with SpatialOMx® workflows on the timsTOF fleX platform.
<h3>14:40 - 15:00 Application Round-up: 4D-Metabolomics™ and 4D-Lipidomics™</h3>
<ul>
<li>Presenter: Dr. Matthias Szesny (Application Scientist Metabolomics, Bruker Daltonics Bremen, Germany)</li>
</ul>
We will highlight the capabilities of the timsTOF platform and introduce new applications, method developments, and software solutions in the field of metabolomics and lipidomics. Those help scientists gain a faster and deeper understanding of diverse research areas such as health and disease as well as agriculture.

Bruker: Expanding the Horizons of 4D-Metabolomics and 4D-Lipidomics

Expanding the Horizons of 4D-Metabolomics and 4D-Lipidomics

Benefits of TIMS for Metabolomics and Lipidomics. SpatialOMx for in-depth 4D-Lipidomics, Application Round-up: 4D-Metabolomics and 4D-Lipidomics.

TBD
<blockquote>
Presenter: Mark Sartain, Ph.D. (LC/MS Applications Scientist, Agilent Technologies, Inc.)
</blockquote>
<blockquote>
Mark has developed a diverse array of targeted and nontargeted mass-spectrometry based metabolomics and lipidomics applications since joining Agilent in 2012, with a focus on complete hardware/software workflows. Mark began utilizing mass spectrometry in his graduate work to characterize glycoproteins, and later established a novel LC/MS strategy to comprehensively profile and identify complex lipids of Mycobacterium tuberculosis in his postdoctoral fellowship at Colorado State University. He continued designing a wide range of MS-based techniques to measure metabolites and lipids for diverse projects as a Research Scientist at the Institute of Systems Biology (Seattle, WA) prior to joining Agilent.
</blockquote>

Agilent Technologies: LC/TQ Solutions to Give Your Lab Multi-omic Biological Insights

LC/TQ Solutions to Give Your Lab Multi-omic Biological Insights

LC/TQ to Give Your Lab Multi-omic Biological Insights

TBD
<blockquote>
Presenter: Mark Sartain, Ph.D. (LC/MS Applications Scientist, Agilent Technologies, Inc.)
</blockquote>
<blockquote>
Mark has developed a diverse array of targeted and nontargeted mass-spectrometry based metabolomics and lipidomics applications since joining Agilent in 2012, with a focus on complete hardware/software workflows. Mark began utilizing mass spectrometry in his graduate work to characterize glycoproteins, and later established a novel LC/MS strategy to comprehensively profile and identify complex lipids of Mycobacterium tuberculosis in his postdoctoral fellowship at Colorado State University. He continued designing a wide range of MS-based techniques to measure metabolites and lipids for diverse projects as a Research Scientist at the Institute of Systems Biology (Seattle, WA) prior to joining Agilent.
</blockquote>

Agilent Technologies: Elucidating Cellular Metabolism with a Full Suite of Next-Generation Omics Tools

Elucidating Cellular Metabolism with a Full Suite of Next-Generation Omics Tools

Cellular Metabolism with a Next-Generation Omics Tools

Join this webinar to hear from Dr Lin Qingsong, Principle Research Fellow, Director, Protein and Proteomics Centre, National University of Singapore and be informed about up-to-date risk assessment considerations of alternative proteins.
About this webinar
Alternative proteins are gaining momentum as a viable and sustainable option to traditional animal-based proteins. In this webinar, we will focus on the applications and potential of omics in key research areas, which drive innovation and food safety in alternative proteins.
Learning points:
<ul>
<li>Be informed about up-to-date risk assessment considerations of alternative proteins</li>
<li>Understand how multi-omics can study novel foods (alternative proteins)</li>
<li>Understand how omics output can help in improving and creating new food safety guidelines to ensure safe alternative proteins for consumers</li>
</ul>
Technical highlights:
<ul>
<li>Protein extraction and proteomics digestion considerations for alternative protein samples</li>
<li>Data processing and databases for discovery proteomics in novel foods</li>
</ul>
<blockquote>
Presenter: Dr Lin Qingsong (Principal Research Fellow (Research Associate Professor), Director, Protein and Proteomics Centre)
</blockquote>
<blockquote>
<ul>
<li>2002 PhD University of Toronto, Canada (major in Clinical Biochemistry)</li>
<li>1994 MSc Xiamen University, China (major in Enzymology)</li>
<li>1991 BSC Xiamen University, China (major in Biochemistry)</li>
</ul>
</blockquote>
<blockquote>
Proteomics and mass spectrometry, Cancer biomarker discovery and cancer biology, Chemical proteomics and drug target identification, Mechanisms of water desalination in mangrove plants and euryhaline fish, Aquaporin biomimetic membrane for water desalination and reuse.
</blockquote>

SCIEX: Omics in the rapidly developing field of alternative proteins: innovation and safety

Omics in the rapidly developing field of alternative proteins: innovation and safety

Join this webinar and be informed about up-to-date risk assessment considerations of alternative proteins.

Omics in developing field of alternative proteins

L-asparaginase (ASNase) is an enzyme-drug that is approved for the treatment of pediatric acute lymphoblastic leukemia (ALL) but is too toxic for adults. To elucidate potentially targetable mechanisms of toxicity with the ultimate goal of decreasing ASNase toxicity and extending its use to adults, we performed multi-omic profiling of the response to ASNase in adult (16-week-old) mice. We administered a range of sub-toxic and toxic doses of ASNase to healthy mice, collected whole blood samples, processed them to plasma, and used a novel sample preparation with just 20 µL mouse plasma as input. We analyzed the extracts using a multi-omic, bioanalytical LC/MS platform capable of measuring 500+ metabolites, 750+ lipids, and 375 peptides.
A Bio-LC was used with three different separations for metabolites, lipids, and peptides. A fast, sensitive, robust, 6495 LC/TQ MS system was used with comprehensive databases for pathway analysis. The results suggested that ASNase induces multi-modal cell death as evidenced by metabolite-, lipid-, and peptide/protein-level changes that occurred in a dose-dependent manner. 
Future studies will test the hypothesis that inhibiting those modes of cell death will decrease ASNase toxicity while preserving anticancer activity. Overall, our findings provide proof-of-concept that multi-omic analysis of drug mechanisms at the protein-, lipid-, and metabolite-levels can unveil toxicity-associated pathways that can be targeted to potentially improve a drug’s therapeutic index.
<blockquote>
Presenter: Ian Edwards (LC/TQ Product Manager, Agilent Technologies, Inc.)
</blockquote>
<blockquote>
Ian holds a Ph.D. from the Centre for Proteome Research at the University of Liverpool.He has spent time as a pre- and post-sales MS applications specialist focused on MS imaging and proteomics, as a field marketing manager for -omics, and as a global pharmaceutical marketing manager. Ian joined Agilent recently as LC/TQ Product Manager.
</blockquote>
<blockquote>
Presenter: Philip Lorenzi, Ph.D. (Associate Professor, Department of Bioinformatics and Computational Biology, The University of Texas MD Anderson Cancer Center)
</blockquote>
<blockquote>
I’m an Associate Professor in the Department of Bioinformatics and Computational Biology at The University of Texas MD Anderson Cancer Center. My laboratory focuses on the development of metabolic therapies for the treatment of cancer (with an emphasis on nutrient metabolism), and I’m also Director of the Proteomics Core Facility and Director of the Metabolomics Core Facility. I’ve co-authored 71 peer-reviewed publications. I co-wrote and was Co-Investigator on a successfully completed $4.5M CPRIT Core Facility Award, managed staff and the budget, and oversaw development of bioanalytical services using current equipment and protocols that we have optimized thoroughly. We’ve developed novel mass spectrometry-based methods for: 1) increasing the accuracy of glutamine and glutamate measurements by minimizing in-source conversion to pyroglutamate; 2) normalizing data based on the DNA content of cell- and tissue-based samples; 3) measuring amino acids from as little as 2 µL of mouse plasma or whole blood; 4) detection of over 2,000 annotated metabolites and lipids per biological sample (including just 2 mg of tissue); 5) stable isotope tracer analyses in vitro and in vivo including methods for measuring energy metabolism; 6) determining the extent and position of 13C incorporation into specific amino acids; and 7) diagnosing and correcting batch effects in metabolomic data. Our multidisciplinary team provides full service contract research in a state-of-the art facility.
</blockquote>

Agilent Technologies: Multi-Omic, Mass Spectrometry-Based Elucidation of Mech. of L-asparaginase Toxicity in a Mouse Model

Multi-Omic, Mass Spectrometry-Based Elucidation of Mech. of L-asparaginase Toxicity in a Mouse Model

We analyzed the extracts using a multi-omic, bioanalytical LC/MS platform capable of measuring 500+ metabolites, 750+ lipids, and 375 peptides.

Multi-Omic, Mass Spectrometry-Based Elucidation of Mech

It’s an exciting time to be a proteomics researcher without a doubt. For years the biggest challenge has been the sheer volume of samples to be analysed. The recent launch of the Thermo Scientific™ Orbitrap™ Astral™ mass spectrometer has promised to be a true game-changer.
For the first time ever, an instrument is available which offers the capability to do high throughput studies of large cohort samples without compromising performance. Join us for this review of presentations from the recent BSPR-EuPA conference showcasing the latest innovations.
Learning points:
<ul>
<li>Latest advances in high throughput proteomics
</li>
<li>Latest advances in large cohort analysis
</li>
<li>Revolutionary instrumentation for deeper proteome coverage
</li>
</ul>
Who should attend:
<ul>
<li>Director, Managers and Researchers in Proteomics
</li>
<li>Director, Managers and Researchers in Cancer Research facilities
</li>
<li>Current users of Orbitrap technology &amp; QTOF MS analysing plasma proteins
</li>
</ul>
<blockquote>
Presenter: Prof Michael MacCoss (Director of MacCoss Lab, University of Washington, Department of Genome Sciences)
</blockquote>
<blockquote>
Michael J MacCoss was born in western Canada to British parents, before relocating to Freehold, New Jersey where he grew up. Mike attended the University of Vermont as an undergrad, receiving a Bachelor of Arts in Chemistry. However, his passion for research only truly came to be after an internship in Dr. Patrick Griffin’s protein mass spectrometry lab at Merck Research Laboratories, and he began pursuing a path in biotechnology.
</blockquote>
<blockquote>
Eventually, Mike obtained a Ph.D. with Professor Dwight Matthews, also at the University of Vermont, and followed that with a post-doc at Scripps Research Institute with Professor John R. Yates III. In 2004 he started the MacCoss lab at the University of Washington with a major emphasis on developing robust and quantitative protein assays.
</blockquote>
<blockquote>
Over the last 14 years, Mike and his team have become leaders in the field of quantitative proteomics. The focus of his lab is the development of methods and software for generating and disseminating quantitative protein assays.
</blockquote>
<blockquote>
Presenter: Dr. Jo Kirkpatrick (Senior Product Specilaist, Thermo Fisher Scientific)
</blockquote>
<blockquote>
Jo has a degree in Chemistry from the University of York and a PhD in analytical chemistry from the University of Reading. Following a post-doc in mass spectrometry in the Chemistry department at Oxford, and working as an application scientist at Waters, she has worked in and ran Proteomics Core Facilities in the UK and Germany, including the EMBL in Heidelberg, the Leibniz Institute on Aging in Jena, The Francis Crick Institute in London and CRUK Cambridge.
</blockquote>
<blockquote>
After many years as an experienced Thermo customer, Jo joined the company earlier this year as a Technical Sales Specialist, supporting the whole of the UK/Ireland, Benelux and Nordic regions, in all things proteomics.
</blockquote>
<blockquote>
When she&#39;s not talking about proteomics and mass spectrometry, Jo enjoys ceroc dancing, tennis, scuba diving, travelling, and spending time with her cats, who like to join in on Teams meetings whenever she works from home.
</blockquote>
<blockquote>
Presenter: Dr. Paul Humphrey (EMEA Senior Regional Marketing Manager, LSMS, Omics and ClinTox, Thermo Fisher Scientific)
</blockquote>
<blockquote>
Paul has a degree in Analytical Chemistry and a PhD in Secondary Ion Mass Spectrometry from the University of Manchester.
</blockquote>
<blockquote>
He previously managed a contract analysis laboratory for several years before moving into a career in the scientific instrument manufacturing industry.
</blockquote>
<blockquote>
Initially an application chemist and product manager he moved into international scientific marketing when he joined Thermo Fisher Scientific in 1997. Since then he has worked in a variety of roles within factory, field marketing and sales office organisations. He has travelled and presented extensively and has been responsible for business in EMEA, North America and Asia/Pacific regions.
</blockquote>
<blockquote>
He lives in the UK and when not working he enjoys travelling, photography, cookery and scuba-diving.
</blockquote>
<blockquote>
Presenter: Robert van Ling (Product Manager, Thermo Fisher Scientific)
</blockquote>
<blockquote>
Robert started his low flow chromatography career as an intern from the Technical School in Amsterdam, The Netherlands, at LC Packings in the mid-90s.
</blockquote>
<blockquote>
Since those early years, Robert has been part of the teams introducing and supporting a wide range of our nano- and capLC products, such as the UltiMate and UltiMate 3000 nanoLC systems, PepMap and EASY-Spray columns. In recent years, he has introduced our new µPAC Neo HPLC column line, an innovative and unique approach to significantly improve the performance and reliability in low flow proteomic separations.
</blockquote>
<blockquote>
Robert still lives in the wider Amsterdam region, and when not talking low flow separations very much enjoys reading fantasy, jigsaw puzzling and listening to prog and hard rock.
 
</blockquote>

Thermo Scientific: Proteomics unleashed: exclusive insights and updates from BSPR-EuPA

Proteomics unleashed: exclusive insights and updates from BSPR-EuPA

Review of presentations from the recent BSPR-EuPA conference showcasing the latest innovations.

Exclusive insights and updates from BSPR-EuPA

Immunopeptidomics is an emerging field that combines proteomics and immunology to study the complex repertoire of peptides presented by major histocompatibility complex (MHC) molecules on the cell surface.
These MHC-bound peptides, known as immunopeptidomes, play crucial roles in immune recognition and activation, influencing various physiological and pathological processes such as immune surveillance, infectious diseases, autoimmunity, and cancer.
Join our webinar to explore recent advancements, challenges, and applications in immunopeptidomics. Discover how Evosep One accelerates discoveries, and support the understanding of immune responses and diseases.
<blockquote>
Presenter: Anthony Purcell (Professor, Purcell Lab, Monsah University)
</blockquote>
<blockquote>
Presenter: Nicolai Bache (Head of Applications at Evosep)
</blockquote>

Advancing Immunopeptidomics

Recent advancements, challenges, and applications in immunopeptidomics.

Immunopeptidomics is a field that combines proteomics and immunology to study the complex repertoire of peptides presented by major histocompatibility complex (MHC) molecules on the cell surface.
These MHC-bound peptides, known as immunopeptidomes, play crucial roles in immune recognition and activation, influencing various physiological and pathological processes such as immune surveillance, infectious diseases, autoimmunity, and cancer.
Join our webinar to explore recent advancements, challenges, and applications in immunopeptidomics. Discover how EvosepOne accelerates discoveries, and support the understanding of immune responses and diseases.
<h4>IMMUNOPEPTIDOMICS ON THE EVOSEP ONE – NEW LEVELS OF SAMPLE THROUGHPUT AND PRODUCTIVITY</h4>
Immunopeptidomics is the study of peptide antigens that are bound to and presented on the cell surface by molecules encoded by the Major Histocompatibility, a highly polymorphic region of the genome that encode molecules involved in immune responses. These peptides are derived from both intracellular and extracellular degradation of the parental proteins, generating a highly complex repertoire of peptide ligands, including peptides derived from pathogens, tissue specific and cancer specific antigens when relevant. In humans, human leukocyte antigen (HLA) class I and class II molecules are of particular interest for immunopeptidomic analysis. These molecules are encoded by several loci and constitute thousands different alleles that vary between individuals. Thus, immunopeptidomes are highly individualized and almost impossible to accurately predict. This predicates the empirical measurement of the complexity and diversity of immunopeptidomes using mass spectrometry. Due to the relatively small amounts of material available for analysis the use of nanoflow LC-MS for immunopeptidome analysis is critical. Here I explore the implementation of the high throughput EvoSEP one platform couples to a Bruker timsTOF Pro 2 for robust analysis of immunopeptidomes across a variety of tissues and cell lines. Using the Whisper 20SPD method data quality and depth is maintained whilst sample carryover is negligible allowing more productive use of instrument time; I highlight significant improvements in throughput with over 1500 immunopeptidomes characterised in just 3 months.
<blockquote>
Presenter: Anthony Purcell (Professor, Purcel Lab, Monsah University)
</blockquote>
<blockquote>
Presenter: Nicolai Bache (Head of Applications at Evosep)
</blockquote>
<h4>MAPPS: High throughput immunopeptidomics for the assessment of the immunogenic potential of protein biotherapeutics</h4>
Biologics, mostly monoclonal antibodies and recombinant proteins, are a class of drugs used to treat some particularly difficult conditions. These proteins, when recognized as non-self by the immune system, can elicit unwanted immunogenicity. One of the first steps in this cascade is the presentation of fragments of this protein by MHC complexes on antigen presenting cells, which might ultimately lead to generation of anti-drug antibodies (ADAs). These ADAs can lower the therapeutic efficiency and can lead to severe immunogenic effects. To bring safe biotherapeutics to the market it is critical to thoroughly assess the immunogenic profile of a biotherapeutic. MAPPS (MHC associated peptides proteomics) assays are the method of choice to define all potential immunogenic regions of a protein. ImmuneSpec, an advanced immunopeptidomics platform, offers MAPPS as a service. Here we show how the combination of high-throughput MHC peptide purification, fast LC using EvoSep, and high sensitive MS addresses these needs.
<blockquote>
Presenter: Kurt Boonen (Assistant Professor, Deparment of biomedical sciences, University of Antwerp)
</blockquote>
<blockquote>
Presenter: Nicolai Bache (Head of Applications at Evosep)
</blockquote>

Evosep: ADVANCING IMMUNOPEPTIDOMICS: LEVERAGING EVOSEP ONE FOR HIGH-THROUGHPUT ANALYSIS AND DISCOVERY

LCMS webinars focusing on OMICS - page 17

ADVANCING IMMUNOPEPTIDOMICS: LEVERAGING EVOSEP ONE FOR HIGH-THROUGHPUT ANALYSIS AND DISCOVERY