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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<h4>Virtual event: Pharma conclave series 2024</h4>
SCIEX offers the platform for the experts to take the stage and drive technological progress
Welcome to Pharma conclave series 2024 – where our customers’ expertise meets innovation, transforming your knowledge and empowering you to revolutionize your work processes. Join us in discovering techniques that will enhance your skills to accelerate your daily operations in the development of new drugs.
From the research of new markers to the drug development moving into non and GLP bioanalysis. Confidently plan your next lab expansion with the knowledge gained from industry leaders and pioneers.
<ul>
<li>May 16 Event 1: Pharma omics</li>
<li>September 17 Event 2: Impurities</li>
<li>October 23-24 Event 3: Pharma</li>
</ul>
10:00 a.m.–12:00 p.m. CET
<h3>Event 2: Impurities</h3>
Impurities in the pharmaceutical industry. What&#39;s next?
While the regulatory landscape is changing faster than ever, having the right information on impurities available to you at every stage of the drug development is vital to bring safe and effective therapies to the market. Whether you want to optimize your lab’s current capabilities or scale up to meet your future demands, this event creates a platform to share the customer’s expertise.
<blockquote>
Presenter: Bruno Manadas, PhD
</blockquote>
<blockquote>
Dr Manadas is a prominent Cell Biology researcher at CNC-UC since 2017. With expertise in biochemistry, psychology, and biotechnology, he&#39;s authored 130+ publications and led multiple projects. As head of CNC&#39;s Mass Spectrometry node and Associate Editor for Frontiers, he&#39;s contributed significantly to neuroscience and psychiatry. Bruno&#39;s research focuses on cell biology mechanisms, translational biomarker research, and MS-based approaches for studying protein oxidation. He played a pivotal role in establishing the hospital biobank and teaches at the Portuguese Catholic University.
</blockquote>
<blockquote>
Presenter: Dorte Bekker-Jensen
</blockquote>
<blockquote>
Dorte is heading the Applications Development team in Proteomics Research at Evosep. She has long-term experience within proteomics and has focused on technology development by developing simple and automated workflows for high-throughput applications.
</blockquote>
<blockquote>
Presenter: Stefan Ledinger
</blockquote>
<blockquote>
Stefan has 20 years of experience in the life sciences and diagnostic industries. For the last dozen years, he has been serving various functions within biocrates life sciences ag. Most recently, he has been responsible for the market development for metabolomics solutions in the pharmaceutical and biotech industries. He currently serves as Global Head of Sales. Stefan holds degrees in business administration and bioengineering, combining commercial know-how with a passion for science.
</blockquote>
<blockquote>
Presenter: Markus Langsdorf
</blockquote>
<blockquote>
Markus has 14 years of experience in life sciences industries. As he joined biocrates in 2010, he worked for 11 years as application support specialist for biocrates’ metabolomics profiling solutions. 3 years ago he changed his position withing the company to his new function as product manager. Markus studied chemistry and graduated with a PhD in Analytical Chemistry.
</blockquote>

Pharma conclave series 2024: Impurities

<h4>Live from the Lab hosted by NIBRT: Solutions for biotherapeutic analysis</h4>
By your side to accelerate your biopharmaceutical development journey
Join us for the second Live from the Lab of 2024, taking place on September 17th, an exciting biopharma hybrid event featuring the latest advancements in separation technology and mass spectrometry. Focusing on all stages of biotherapeutics development, from discovery and research, all the way to routine and QC analysis, this event will give you valuable insights to accelerate your biopharmaceutical development journey.
The following speakers will talk at this event at the NIBRT research facility which will be streamed live all over Europe:
<ul>
<li>Dr. Jonathan Bones, NIBRT</li>
<li>Prof. Mark Dickman, University of Sheffield</li>
<li>Dr. Dan Bach Kristensen, Symphogen</li>
<li>Dr. Mark Hilliard, Pfizer</li>
<li>Dr. Ken Cook, Thermo Fisher Scientific</li>
<li>Jon Bardsley, Thermo Fisher Scientific</li>
</ul>
Whether you are a researcher, scientist, or industry professional in our region, this biopharma event is not to be missed. Expand your knowledge, network with experts, and discover how the Thermo Scientific solutions will stand by your side to accelerate your biopharmaceutical development journey.
Mark your calendars for September 17th and join us for this impactful hybrid event foster collaboration within the scientific community.
Participation is free of charge, registration is required.
For any questions about this event or regarding your registration, please email CMDEvents@thermofisher.com.
<h4>How to attend?</h4>
3 ways of attending:
<h5>Online attendees (remote):</h5>
Unable to travel to a satellite? Not a problem! You can register to attend conveniently online from your desk or anywhere else through the live stream from NIBRT.
<ul>
<li><a href="https://assets.thermofisher.com/TFS-Assets/CMD/Flyers/fl-003119-pb-live-from-the-lab-ms-biotherapeutics-agenda-online-fl003119-em-en.pdf">Agenda</a></li>
</ul>
<h5>NIBRT Research Facility (in-person event):</h5>
Join the heart of the event where the main agenda will be hosted and live streamed across our region to our satellite events and our online audience. Attendance through VIP invitation only!
<h5>Join a ‘Satellite’ location (in-person event):</h5>
Across Europe, our in-person satellite events will be broadcasting the main agenda live streamed from NIBRT, Dublin and supplement the day with local speakers/lab tours pending on the satellite. Take this opportunity to network with fellow scientists and meet your Thermo Fisher representatives from technical, commercial, and service functions. Check out the closest location to you and their individual agenda!
<ul>
<li>Søborg, Denmark (AGC Biologics)</li>
<li>Dreieich, Germany (Thermo Fisher Scientific)</li>
<li>Segrate, Italy (MI) (Thermo Fisher Scientific S.P.A.)</li>
<li>Leiden, Netherlands (Janssen Biologics BV)</li>
<li>Ljubljana, Slovenia (Four Points by Sheraton Ljubljana Mons)</li>
<li>Reinach, Switzerland (Thermo Fisher Scientific)</li>
<li>Hemel Hempstead, UK (Thermo Fisher Scientific)</li>
</ul>

Thermo Fisher Scientific: Live from the Lab: Solutions for biotherapeutics

Live from the Lab: Solutions for biotherapeutics

An exciting biopharma hybrid event featuring the latest advancements in separation technology and mass spectrometry.

The sample throughput of high-sensitivity liquid chromatography-mass spectrometry (LC-MS) based proteomics analysis is restricted by the pressure limitations of LC and column hardware, with some methods wasting as much as 50% of the method cycle time outside of MS acquisition.
Traditional routes for boosting throughput include shorter columns and gradients, higher flow rates, and using trap-and-elute workflows – all of which introduce trade-offs in sensitivity and proteome depth.
The Thermo Scientific™ Vanquish™ Neo tandem direct injection workflow leverages hardware innovations and software intelligence to eliminate method overhead while maintaining data quality across nano, capillary, and micro-flow LC-MS.
In this webinar experts from Evotec and Bayer will showcase how they implemented the tandem direct injection workflow for their proteomics work. Dr. Nagarjuna Nagaraj will present on how Evotec is using tandem direct injection with nano-LC columns packed in-house to boost sample throughput of their chemoproteomics screening pipeline, while Dr. Alexander Boychenko from Bayer will discuss how his lab is using a micro-flow tandem direct injection approach to analyze plasma samples for translational proteomics.
Learning Objectives
<ul>
<li>See how minimizing LC-MS method overhead can accelerate sample throughput while maintaining proteome depth
</li>
<li>Discover how labs are using tandem direct injection for chemoproteomics and translational proteomics applications
</li>
<li>Learn how to implement tandem direct injection in your proteomics workflow
</li>
</ul>
<blockquote>
Presenter: Dr. Nagarjuna Nagaraj (Group Leader High Sensitivity Proteomics, Evotec)
</blockquote>
<blockquote>
Dr. Nagarjuna Nagaraj is a proteomics group leader at Evotec focusing on high sensitivity and high throughput proteomics applications with more than 18 years of experience in proteomics and mass spectrometry. Nagarjuna obtained his PhD from the Matthias Mann lab focusing on sample preparation and MS data acquisition strategies for clinical applications. After a postdoc he directed the mass spectrometry core facility at the Max-Planck-Institute of Biochemistry working on a wide range of protein and peptide mass spectrometry projects such as bottom-up proteomics, structural mass spectrometry including HDX, native and crosslinking MS, intact protein and small molecule analysis.
</blockquote>
<blockquote>
Presenter: Dr. Alexander Boychenko (Head of R&amp;D Laboratory Precision Medicine Markers, Bayer)
</blockquote>
<blockquote>
Alexander Boychenko is leading Omics Research within the Translational Sciences team of the Pharmaceuticals division at Bayer Group. He is focused on implementing innovative analytical technologies and developing novel methodologies for proteomics, metabolomics, and ligand-binding assays (LBA) to comprehensively characterize human and animal model phenotypes, enabling disease understanding and novel biomarker discovery. He holds a Ph.D. in Analytical Chemistry from Kharkiv National University, Ukraine. During his post-doctoral work at the University of Groningen, The Netherlands, he combined LC-MS and immunoassays to discover and validate protein biomarkers in biofluids for cancer screening. Before joining Research and Early Development at Bayer AG, he developed and introduced new liquid chromatography-mass spectrometry products at Thermo Fisher Scientific. Alexander is a subject matter expert in LC-MS, biological data interpretation, and precision medicine. He utilizes his passion for applying technical expertise to develop new medicines.
</blockquote>
<blockquote>
Presenter: Dr. Alec Valenta (Product Marketing Manager, Thermo Fisher Scientific)
</blockquote>
<blockquote>
Alec is the product marketing manager for the Vanquish Neo UHPLC system and low-flow LC columns. Prior to joining Thermo Fisher Scientific he earned his PhD in analytical chemistry from the University of Michigan where he helped advance microdialysis sampling of neurochemicals and developed LC-MS methods to quantify small molecule neurotransmitters, neuropeptides, and metabolites in a variety of complex biological samples.
</blockquote>

Thermo Scientific: A Tandem LC Workflow for Maximizing Mass Spectrometer Utilization in Proteomics

A Tandem LC Workflow for Maximizing Mass Spectrometer Utilization in Proteomics

How experts from Evotec and Bayer implemented the tandem direct injection workflow for their proteomics work.

A Tandem LC Workflow for Maximizing Mass Spectrometer

Join us for an exclusive two-day event where Agilent will showcase cutting-edge biopharma solutions.
The first day of the event we will explore Agilent’s comprehensive portfolio for the spectrum of applications from drug discovery to quality control. Learn more about our cell analysis and genomics expertise and the tools we provide to drive IVT mRNA development, protein therapeutics and cell and gene therapies
The second day will focus on advanced analytical solutions, including HRMS for tRNA sequencing and LC/MS for DNA/RNA analysis. Learn how to scale up oligonucleotide purification with Agilent biocolumns, which enhance the efficiency and accuracy of your processes.
By attending this event you will:
<ul>
<li>Gain insights from Agilent to optimize biotherapeutic workflows, including rigorous quality testing in cGMP environments and handling nucleic acid, vaccines, mAB and protein samples.
</li>
<li>Understand how metabolic analyses can impact CAR cell function and behavior, using cytolytic cell killing assays on the xCELLigence system to develop cell therapy processes and confirm product potency.
</li>
<li>Learn about new techniques in high-resolution LC/MS for analyzing tRNA modifications.
</li>
<li>Discover software tools available for high-resolution MS systems in both research and QA/QC labs.
</li>
<li>Compare analytical and semipreparative LC purification methods for synthetic oligonucleotides, gaining competitive insights into purification strategies.
</li>
</ul>
<h5>Talk 1: Agilent Tools and Technologies to Drive Advancements in Biopharmaceutical Drug Development</h5>
<ul>
<li>Presented by Dr. Hervé Chaulet, Molecular and Biological Research Market Specialist, Agilent Technologies</li>
</ul>
Discovering, developing, and manufacturing biopharmaceuticals requires you to stay abreast of advances in knowledge and improvements in technology while constantly navigating a maze of business and scientific challenges. Agilent can be a trusted partner providing expertise and end-to-end workflows including systems, software, consumables, and services for the spectrum of applications from drug discovery to quality control. Learn more about our cell analysis and genomics expertise and the tools we provide to drive IVT mRNA development, protein therapeutics, and cell and gene therapies.
<h5>Talk 2: Quality Control In IVT mRNA Therapeutics and Vaccine Development Workflow Using The Agilent Fragment Analyzer System</h5>
<ul>
<li>Presented by Dr. Leslie Friedmann, Product Manager, Agilent Technologies</li>
</ul>
Reliable and robust analysis is essential throughout in vitro transcription (IVT) mRNA workflows, providing important quality information to help minimize risk and aid in the production of a consistent product. The Agilent Fragment Analyzer systems can be used for several QC steps at different checkpoints in mRNA vaccine development, providing accurate and precise sizing and integrity analysis. These QC steps are to determine the quality and size of the linearized plasmid, the size and purity of the IVT mRNA, length of the poly(A) tail, and purity of the final mRNA vaccine product.
<h5>Talk 3: Analysis of NIST mAb Reference Material by Parallel SDS-Capillary Electrophoresis</h5>
<ul>
<li>Presented by Dr. Kyle Luttgeharm, Product Manager, Agilent Technologies</li>
</ul>
Monoclonal antibody drug products are complex biomolecules that must be tested for critical quality attributes (CQAs) such as monomeric purity and percent glycosylation. Capillary gel electrophoresis methods have been adopted as the standard method for size heterogeneity characterization, however legacy capillary electrophoresis (CE) methods involve complicated workflows or are cost prohibitive. To address these problems with legacy methods, Agilent has developed a 12-channel, parallel capillary electrophoresis-SDS (CE-SDS) instrument and reagents. The system uses a high-resolution sieving gel, allowing for resolution of mAb species including the non-glycosylated heavy chain and light chain. To demonstrate the capabilities of the ProteoAnalyzer, the NIST mAb was characterized under both reduced and non-reduced conditions and compared to the NIST data sheet.
<h5>Talk 4: Advanced Analytics for Cell Therapy Research, Process Development, and Manufacturing</h5>
<ul>
<li>Presented by Dr. Kelly Kroeger, Science &amp; Technology Advisor, Agilent Technologies</li>
</ul>
With immunology and immune-based therapies rising as a pillar of science and therapeutics, we are seeing a foundational shift from targeting specific proteins and pathways to actually targeting the immune cellular network that resolves and prevents disease. Therefore there is a critical need for cell analysis tools to facilitate understanding of the dynamic nature of the interaction of these cellular networks whether it is in the context of immune cells or immune cells with cancer cells.
To address these new challenges, we at Agilent Technologies have developed a portfolio of cell analysis solutions that provide researchers with more relevant tools to measure living cells, dynamically track them, and model their microenvironments. These next-generation therapies require methods and technologies to enable assessment of real-time cell function, phenotype, and fate. Used together, the Agilent tool bench provides the capability to measure and develop immune cell function more effectively, thus enabling translational researchers and developers to achieve the necessary level of potential therapeutic potency and safety.

Technology Networks: Biopharma Innovations Summit

Biopharma Innovations Summit Day 1

Learn more about our cell analysis and genomics expertise and the tools we provide to drive IVT mRNA development.

With the timsTOF Pro, powered by the PASEF® acquisition modes, Bruker has largely contributed to take proteomics analysis to a new dimension, by removing the need to compromise speed for sensitivity or selectivity, while reaching unprecedented levels of robustness.
Introduced @ ASMS 2024, the timsTOF Ultra 2 is the pinnacle of timsTOF evolution, combining ultimate sensitivity, speed, selectivity and dynamic range with the field-proven legendary timsTOF robustness. During this live from the lab, you will witness through real-life examples how sensitive and versatile the timsTOF Ultra 2 can be.

Bruker: Taking 4D-Proteomics™ to the routinely exceptional with the timsTOF Ultra 2j

Taking 4D-Proteomics™ to the routinely exceptional with the timsTOF Ultra 2

Through real-life examples how sensitive and versatile the timsTOF Ultra 2 can be.

Taking 4D-Proteomics™ to the routinely exceptional

Fragmentation-based molecular annotations are the gold standard in high-confidence biomarker identification using mass spectrometry.
The new iprm-PASEF workflow integrates CCS-enabled MALDI Imaging of lipids with a targeted MS/MS imaging approach that allows spatial fragmentation and analysis of multiple targets in a single acquisition. The workflow includes a fully integrated pipeline within our software ecosystem to generate accurate identifications with spatial fidelity.
Key Learning Objectives:
<ul>
<li>Fragmentation based MALDI Imaging capabilities
</li>
<li>iprm-PASEF workflow for the timsTOF fleX
</li>
<li>Fragmentation based annotation pipeline using SCiLS™ Lab
</li>
</ul>
Who should attend:
<ul>
<li>Researchers interested in expanding their spatial biology toolkit
</li>
<li>Researchers focused on maximizing confidence of molecular annotations for MALDI Imaging
</li>
<li>Anyone who wants to expand their MALDI Imaging workflows
</li>
</ul>
<blockquote>
Presenter: Michael Becker, Ph.D. (Principal Scientist DMPK, Boehringer Ingelheim Pharma GmbH &amp; Co KG, Mainz, Germany)
</blockquote>
<blockquote>
Dr. Michael Becker is the head of the Mass Spectrometry Imaging lab at Boehringer Ingelheim. He received his Ph.D. in Neurobiology, and transitioned into the imaging field more than 15 years ago. He uses MSI to study drugs and drug-induced changes in tissue. To do so, he tries to push the sensitivity, reproducibility and specificity of the method.
</blockquote>
<blockquote>
Presenter: Arne Behrens, Ph.D. (Application Specialist in MALDI Imaging, Bruker Daltonics GmbH &amp; Co. KG, Bremen, Germany)
</blockquote>
<blockquote>
Dr. Arne Behrens is an Imaging Applications Scientist  at Bruker in Bremen with more than 6 years of experience on the timsTOF fleX platform. He received his Ph.D. in Analytical Chemistry and is an expert for CCS-enabled MALDI Imaging applications.
</blockquote>
<blockquote>
Presenter: Björn Wendik, Ph.D. (Business Development Manager, Bruker Daltonics GmbH &amp; Co. KG, Bremen, Germany)
</blockquote>
<blockquote>
Björn studied biology at the University of Würzburg and University of Freiburg with focus on developmental biology. In Freiburg he did his Ph.D. working on motoneuron development and pancreas formation. He became an expert on life cell imaging, timelapse studies and 3d-image software analyses. He continued his work as lecturer at the University of Freiburg where he also took care of parts of the Imaging core facility. When stepping into industry, he worked as a specialist for confocal microscopy and from there moved on into multispectral imaging, antibody based multi- and hiplexing and tissue analysis platforms. With this expertise, Björn started as a Business Development Manager for the MALDI Imaging at Bruker in July 2023.
</blockquote>

Bruker: Confidence in spatial identifications using iprm-PASEF on the timsTOF fleX

Confidence in spatial identifications using iprm-PASEF on the timsTOF fleX

The new iprm-PASEF workflow integrates CCS-enabled MALDI Imaging of lipids with a targeted MS/MS imaging approach.

Confidence in spatial identifications using iprm-PASEF

<h3>Session #1 - Advancements in Targeted Quantitation of PFAS</h3>We are thrilled to invite you to our upcoming webinar focused on enhancing laboratory efficiency and accuracy in PFAS analysis. Join us to explore innovative solutions that streamline processes and improve detection capabilities.1. Harnessing the Power of Mass Spectrometry and Automation to Reduce Sample Size, Sample Preparation Time and Increase Laboratory Efficiency of PFAS Analysis for EPA 1633<ul><li>Presented by Kari Organtini</li></ul>EPA Method 1633 is widely used for analyzing PFAS in non-potable water, soils, biosolids, and tissues. This presentation will show how advanced mass spectrometry and automation can significantly reduce sample size, cut down preparation time, and boost overall laboratory efficiency.2. Identification of short chain per and polyfluorinated alkyl substances (PFAS) using ion ratios with low mass product ions<ul><li>Presented by Stuart Adams</li></ul>As long-chain PFAS are replaced by short and ultrashort-chain alternatives, their detection becomes more challenging. This talk will cover how modified tandem quadrupole mass spectrometry enhances sensitivity, enabling the identification of these difficult-to-detect PFAS compounds using low-mass product ions.3. Evaluation of DESI mounted on Q-TOF and TQ mass spectrometers to image PFAS compounds in different matrices<ul><li>Presented by Emmanuelle Claude</li></ul>Direct analysis with minimum sample preparation as well spatial dimension of PFAS in samples can add simplicity and localization information, to complement state of the art detection and quantification by UHPLC-MRM analysis. Results are presented to evaluate the level of detection of few tens of PFAS compounds that were spotted on porcine liver tissue section, after updating the DESI imaging workflow to minimize external contamination. Several mass spectrometers such as discovery workflow in full scan TOF mode on the MRT and Cyclic mass spectrometers as well as targeted workflow using MRM acquisition mode on the DESI XS Xevo TQ Absolute MS were compared. Finally the benefit of ion mobility separation for the MSI analysis of PFAS is described. 61% and 55% of the PFAS compounds were detected as low as 10 ng/mL spotted on tissue when analyzed by negative mode DESI in discovery full scan MS acquisition mode. The targeted MRM workflow is the most sensitive system with 77% of the PFAS compounds detected as low as 10 ng/mL spotted on tissue.Join us to learn how these technologies are transforming PFAS analysis, helping laboratories meet the growing demand for more efficient and accurate testing.<blockquote>Presenter: Dr. Stuart Adams (Principal Scientist, Market Development, Food and Environmental Applications, Europe, Waters Corporation)Stuart has been developing methods for the determination of contaminants in food and the environment for over 17 years and has been with Waters Corporation since 2018. Stuart's previous role was as a senior analytical chemist at Fera (the UK’s National Reference Laboratory) and moved to Waters to focus on application development in the European region. He now serves as the attached scientist to the European Market Development team responsible for the food and environmental application areas. In his role, he works with customers to understand their analytical challenges and helps address them with Waters technologies.Presenter: Kari Organtini, Ph.D. (Principal Scientist, Food &amp; Environmental, Waters Corporation)Kari Organtini is a senior scientist at WatersCorporation and has been with the company for five years. She received her PhD from Penn State University in 2015 studying the occurrence of dioxins and furans in fire debris and their implications to first responder health. At Waters, Kari is part of the food and environmental applications team. Kari has developed applications using both LC and GC techniques for a variety of applications ranging from pesticides to persistent organic pollutants during her career. She is currently the scientific lead for developing PFAS applications at Waters.Presenter: Emanuelle Claude (Consulting Scientist D&amp;C Imaging, Waters Corporation)Miss Emmanuelle Claude (Master in Fine Chemistry and Business and M.Phil in spectroscopy analysis in organic chemistry and biology) is currently a Consulting scientist in the Scientific Operations Department, Wilmslow, UK.She started at Waters Corporation in October 2000 as an Application Chemist in the Proteomics and Genomics Marketing group, developing automated Peptide Mass Fingerprint (PMF) MS methods using a MALDI-TOF mass spectrometer.Over the years she developed several methods in the proteomics analytical space using MALDI TOF and naturally moved in starting the development of Mass Spectrometry Imaging (MSI) at Waters corporation over 15 years ago.She has been involved with hardware and software R&amp;D to ensure that the solutions are fit-for-purpose for the MSI community and beyond. She has worked extensively with the main MSI leaders in Europe and the US such as Prof Heeren in the Netherlands, Prof Clench, Prof Takats and Bunch in the UK and Prof Caprioli in the US. She has been a Principal Scientist since 2014 and became a Consulting scientist in 2021 and is part of the MS imaging application team at Waters where data are generated for collaborations and marketing activities (i.e. application literature, customer presentation, papers, posters...), hardware and software requirements are defined for the R&amp;D teams. The team evaluates and develops new applications &amp; methods for imaging by both MALDI and DESI mass spectrometry, support sales with customers visit and demonstration laboratory worldwide.Presenter: Ken Rosnack (Principal Market Development Manager, Waters Corporation)Ken Rosnack is a Principal Market Development Manager in the Testing &amp; Lab Services Group for Waters Corporation. His primary focus is within regulated and routine LC-MS/MS environmental market where he is responsible for world-wide strategy implementation and performance. He maintains collaborations within regulatory agencies as well as with global industrial partners. Over his career, Ken has been primary author on numerous publications, been an invited speaker multi-nationally, and has presented at many conferences. He has been involved with MS for the past 40 years.</blockquote>

Waters Corporation: Advancements in Targeted Quantitation of PFAS

Advancements in Targeted Quantitation of PFAS

Learn how technologies are transforming PFAS analysis, helping laboratories meet the growing demand for more efficient and accurate testing.

<h3>Session #2 - Innovative Approaches in HRMS and Software for PFAS Analysis</h3>We are excited to invite you to our upcoming webinar, where we will explore the latest advancements in PFAS analysis through innovative screening methods and technologies. Our expert speakers will cover various approaches to enhance the detection and identification of per- and polyfluoroalkyl substances (PFAS).<h4>1. Nontarget Screening workflow (NTS) for the Analysis of Per and Polyfluoroalkyl Substances (PFAS) using High resolution mass spectrometry (HRMS)</h4><ul><li>Presented by Hania Khoury-Hollins</li></ul>This session will focus on using HRMS as an effective tool to detect both regulated and non-regulated PFAS. We’ll explore the UNIFI™ screening workflow and discuss the use of comprehensive PFAS libraries to improve detection capabilities.<h4>2. Untargeted Screening for PFAS Chemicals Using Comprehensive Feature Detection</h4><ul><li>Presented by Jeff Goshawk</li></ul>Discover how advanced feature detection methods can identify a wide range of PFAS chemicals, including those not covered by traditional reference standards. This talk will highlight techniques to detect novel PFAS-like chemicals, providing a broader understanding of total organic fluorine content in samples.<h4>3. Elevating Specificity and Identification Confidence for PFAS Liquid Chromatography and Cyclic Ion Mobility Mass Spectrometry</h4><ul><li>Presented by Michael McCullagh</li></ul>Learn how cyclic ion mobility (cIM) enhances the separation and identification of PFAS isomers. By using this method, we can achieve greater specificity and reduce analysis time, providing insights into PFAS exposure and its potential health impacts.Join us to learn how these cutting-edge approaches are revolutionizing PFAS detection and analysis, offering more accurate and efficient solutions for environmental monitoring and public health protection.<blockquote>Presenter: Hania Khoury-Hollins (Principal Scientist, Waters Corporation)Hania Khoury-Hollins is a scientist and researcher at Waters Corporation. She holds a bachelor’s degree in science, which laid the foundation for her scientific pursuits. In 2001, Hania earned her master’s degree in Toxicology, deepening her understanding of the impact of chemicals on living organisms. In 2005 she successfully defended her Ph.D. in physical chemistry from University René Descartes - Paris V (France). After undertaking several different projects in academia Hania spent some time working at Agilent before joining Waters.At Waters, her work revolves around developing cutting-edge analytical techniques and their applications with a focus on Liquid Chromatography coupled with High-Resolution Mass Spectrometry (LC-HRMS). Her expertise encompasses a diverse range of applications, including drug development, proteomics, metabolomics, and lipidomics. More recently, Hania has been developing applications strategies for per- and polyfluoroalkyl substances (PFAS).Presenter:&nbsp;Mike McCullagh (Consulting Scientist, Waters Corporation)Michael has worked at Waters Corporation for over 23 years. His main focus has been non-targeted analysis using time of flight mass spectrometry and ion mobility mass spectrometry. Michael has made contributions to various teams, including Food and Environmental, MS Evaluation, Life Science, Scientific Operations, the Advanced Mass Spectrometry Team and currently in Research, Development and Advanced Testing. Research has been performed across multiple application areas including, impurity profiling, pesticide screening, natural products, food analysis, metabolite identification and more recently non-targeted PFAS analysis. Having worn a number of different “hats”, the common thread has been the privileged opportunity to work with new technologies, new informatics solutions and to collaborate with industry and global collaborative partners, to forge a path to new discoveries and contribute to solutions to analytical challenges across multiple disciplines.Presenter:&nbsp;Jeff Goshawk (Consulting Scientist, Waters Corporation)Jeff is a Consulting Scientist at Waters Corporation and has been with the company for twenty-four years. Jeff started his career at Waters as a software developer working on MassLynx and its associated application managers. Jeff subsequently transitioned into the applications development group where he joined the toxicology team as a Principal Scientist. Jeff is now back in the software development world at Waters, and is currently working on the Pattern Analysis Application.Presenter:&nbsp;Frank L. Dorman, PhD, FRSC (Principal Environmental Market Manager, Waters Corporation)Frank Dorman is currently Senior Business Development Manager for Waters focusing on their global environmental business and, concurrently, Associate Professor (adjunct) in the Department of Biochemistry and Molecular Biology (BMB) at Penn State University in University Park, PA. In his role at Waters, Frank manages the research-focused environmental market, external collaborations and also interfaces with R&amp;D for new product development. Prior to Waters, Frank was employed full-time as a tenure-line Faculty member of Penn State and served as a member of the Graduate Faculty in: Biochemistry, Microbiology and Molecular Biology (BMMB), Chemistry (CHEM) and the Programs in Forensics Science (FRNSC), and Biogeochemistry (BGC). Frank is also a member of the Center for Molecular Toxicology and Carcinogenesis at Penn State. Frank’s scientific interests are in gas and liquid chromatography fundamental characterization, instrumentation and column development, as well and mass spectrometry and atomic spectroscopy as applied to trace analysis in complex sample matrices. This work is directed towards environmental forensics, traditional forensic chemistry and where environmental exposure events may contribute to human disease; an area sometimes referred to as “exposomics”.Prior to joining the faculty at PSU, Frank was at Restek Corporation for 14 years as the Director of Technical Development, and R&amp;D Senior Chemist. During most of this same time, Frank was also an Adjunct Research Professor at Juniata College where he maintained an active undergraduate research program. Prior to that he was at Inchcape Testing Services for 5 years as a Senior Chemist, Organics Section Manager for Sample Preparation and Corporate Methods Development Chemist. As such, Frank has extensive experience in both the Industrial and Academic sectors giving him a relatively rare combination of skills and experience.</blockquote>

Waters Corporation: Innovative Approaches in HRMS and Software for PFAS Analysis

Innovative Approaches in HRMS and Software for PFAS Analysis

Learn how these cutting-edge approaches are revolutionizing PFAS detection and analysis, offering more accurate and efficient solutions.

<div class="summary-section section" style="-webkit-text-stroke-width:0px;background-color:rgb(255, 255, 255);box-sizing:border-box;color:rgb(51, 51, 51);font-family:&quot;Segoe UI&quot;, Frutiger, &quot;Frutiger Linotype&quot;, &quot;Dejavu Sans&quot;, &quot;Helvetica Neue&quot;, Arial, sans-serif;font-size:14px;font-style:normal;font-variant-caps:normal;font-variant-ligatures:normal;font-weight:400;letter-spacing:normal;margin-bottom:34px;orphans:2;text-align:start;text-decoration-color:initial;text-decoration-style:initial;text-decoration-thickness:initial;text-indent:0px;text-transform:none;white-space:normal;widows:2;word-spacing:0px;">This interactive session will bring together the MS community to discuss some of the most popular and exciting peer-reviewed publications in a friendly and open forum. Ahead of each meeting, we will send out a link to the discussion article, then during the session an expert will summarise the main findings and answer your questions.<h5 style="margin-left:0px;">Be prepared make sure you read&nbsp;<a style="box-sizing:border-box;color:rgb(66, 139, 202);text-decoration:none;user-select:auto;" target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acscentsci.0c00049" fr-original-style="">Native Mass Spectrometry Can Effectively Predict PROTAC Efficacy</a></h5>We're going to be joined by Dr Rebecca Beveridge from the University of Strathclyde, a senior lecturer with a host of experience with development of native ion mobility mass spectrometry methods to study proteins and protein complexes&nbsp;This paper describes how Waters' SYNAPT MS can be utilized&nbsp;demonstrate the strength of native mass spectrometry to delineate the complex binding mechanisms of protein degraders, involving the formation of three-component protein−ligand complexes.<h5 style="margin-left:0px;">Reasons to Attend:</h5><ul style="box-sizing:border-box;margin-bottom:10px;margin-top:0px;"><li style="box-sizing:border-box;">Debate some of the most topical papers from all-time favourites to some of the latest releases &nbsp;</li><li style="box-sizing:border-box;">Focus on understanding the benefit of SYNAPT MS and how to get the most out of the system for native mass spectrometry and biomolecule analysis &nbsp;</li><li style="box-sizing:border-box;">Gain a greater understanding of applications and technologies by asking questions of the authors and/or expert panel &nbsp;</li><li style="box-sizing:border-box;">No pre-recorded content, authors will be LIVE and on camera to answer questions</li></ul>Abstract&nbsp;Protein degraders, also known as proteolysis targeting chimeras (PROTACs), are bifunctional small molecules that promote cellular degradation of a protein of interest (POI). PROTACs act as molecular mediators, bringing an E3 ligase and a POI into proximity, thus promoting ubiquitination and degradation of the targeted POI. Despite their great promise as next-generation pharmaceutical drugs, the development of new PROTACs is challenged by the complexity of the system, which involves binary and ternary interactions between components. Here, we demonstrate the strength of native mass spectrometry (nMS), a label-free technique, to provide novel insight into PROTAC-mediated protein interactions. We show that nMS can monitor the formation of ternary E3-PROTAC-POI complexes and detect various intermediate species in a single experiment. A unique benefit of the method is its ability to reveal preferentially formed E3-PROTAC-POI combinations in competition experiments with multiple substrate proteins, thereby positioning it as an ideal high-throughput screening strategy during the development of new PROTACs<div style="box-sizing:border-box;clear:both;">&nbsp;</div><div class="speaker-fields-container" style="box-sizing:border-box;padding-top:5px;"><div class="section" style="box-sizing:border-box;margin-bottom:34px;"><div class="sp-begin" style="box-sizing:border-box;clear:both;color:rgb(0, 0, 0);font-size:14px;"><blockquote><div style="box-sizing:border-box;">Presenter: Dr Rebecca Beveridge (Senior Lecturer, University of Strathclyde)</div><div style="box-sizing:border-box;">&nbsp;</div><div style="box-sizing:border-box;">Rebecca is a Senior Lecturer and UKRI Future Leaders Fellow who joined the University of Strathclyde in June 2020 as a Chancellor's Fellow. She obtained a BSc in biochemistry and chemistry from the University of Leeds in 2011 and completed her PhD at the University of Manchester in 2015. Rebecca spent 4 years at the Institute for Molecular Pathology in Vienna, Austria as a postdoctoral researcher/ Lise Meitner Postdoctoral Fellow. Throughout her career, she has collected experience in a plethora of mass spectrometry methods to study protein structure such as native mass spectrometry, ion mobility, hydrogen-deuterium exchange, and crosslinking.</div>Rebecca’s current research is centered around the development of native ion mobility mass spectrometry methods to study proteins and protein complexes, particularly those that are challenging to study with conventional biochemistry methods.Such systems include intrinsically disordered proteins that exist in a wide range of different shapes, and protein complexes formed by protein-degrading molecules such as PROTACs, the complex binding modes of which are challenging to delineate.</blockquote></div></div></div></div>

Waters Corporation: Native Mass Spectrometry Can Effectively Predict PROTAC Efficacy

Native Mass Spectrometry Can Effectively Predict PROTAC Efficacy

Discuss some of the most popular and exciting peer-reviewed publications in a friendly and open forum.

Native Mass Spectrometry Can Effectively Predict PROTAC

<h4>The Waters 2024 Virtual Summer School - An Educational Journey to Master Food &amp; Environmental Analysis</h4>Unlock the full potential of LC-MS techniques with our immersive and educational sessions at the Waters Virtual F&amp;E Late Summer School 2024. From September 24th to 26th, engage with leading experts and discover cutting-edge methods for environmental and food analysis.<h5>Why attend?</h5><ul><li>Comprehensive Learning: Dive deep into advanced LC-MS techniques and gain practical knowledge to enhance your laboratory's analytical capabilities.</li><li>Expert Insights: Learn from industry leaders and gain firsthand experience through detailed modules on chromatography, mass spectrometry, and sample preparation.</li><li>Regulatory Compliance: Stay ahead with the latest insights on EU regulations for PFAS analysis in food and water, ensuring your lab meets stringent standards.</li></ul><h3>Episode #3: Introduction Non-target Screening (NTS) | F&amp;E Summer School - Day 1 - Module 3</h3>Suspect and non-target screening (NTS) are crucial techniques used in various fields, including food analysis, environmental studies, toxicology, and doping analysis. In this overview, we’ll discuss a holistic approach and introduce high-resolution mass spectrometry methods for both Suspect and NTS screening. Topics covered include resolution, accurate mass data, and ion mobility.In an ideal scenario, Suspect screening and non-Target screening are closely interconnected. Prior knowledge about a potential analyte (Suspect) can expedite the non-Target screening process. We’ll briefly explore Suspect screening and how high-resolution mass spectrometry offers identification criteria for confidently identifying suspect compounds.Further, we examine the data gathered for non-target compounds through high-resolution mass spectrometry. In this module we give a concise introduction to the valuable data that can be compiled for assigning structures. In the forthcoming module 4b we will delve into how this data, in conjunction with the tools offered by the waters_connect software, can be conveniently accessed by the user and provide more comprehensive insights.<h5>What you'll learn:</h5><ul><li>What is Screening? (Target/ Suspect &amp; Non-Target Screening)</li><li>Basics of HRMS (Resolution and accurate mass)</li><li>Identification criteria for Targets /Suspects &amp; UNIFI Scientific Library</li><li>Tools for Non-Target Screening</li><li>Short introduction of exemplary instrument types</li><li>Xevo G3 QToF for Routine Screening</li><li>Xevo MRT for Screening with very high-resolution and very high mass accuracy</li><li>Select Series Cyclic IMS for Screening with ion-mobility utilizing CCS-values</li></ul><blockquote>Presenter:&nbsp;Christoph Thomas (Principal Sales Applications Chemist, Waters Corporation)Christoph Thomas is a Principal Sales Applications Chemist from the Central Europe Customer Success Team based in Eschborn, Germany. He has more than 25 years’ experience in the field of Chromatography and Mass Spectrometry and is familiar with several application areas using Quadrupole and Tof instruments. Within the last decade his projects were mainly focused on the waters_connect Screening Solution in food and environmental screening, toxicology screening, metabolite identification and in the field of extractables and leacheables.Presenter:&nbsp;Gunnar Weibchen (Principal MS Sales Dev Specialist, Waters Corporation)Gunnar studied Chemistry and obtained a PhD in Organic and Analytical Chemistry in Hamburg. After working as an Application Chemist in the demo laboratory at Varian, has been with Waters in Sales and Marketing since 2010</blockquote>

Waters Corporation: The Waters 2024 Virtual Summer School

Introduction Non-target Screening (NTS)

We’ll discuss a holistic approach and introduce high-resolution mass spectrometry methods for both Suspect and NTS screening.

LCMS webinars focusing on LC/HRMS - page 21