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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Biomonitoring of toxicants like pesticides and PFAS in humans is essential for understanding how chemical exposure affects our health, yet chemical coverage is currently limited with targeted LC-MS approaches.Untargeted data acquisition, however, is emerging as a promising tool for broader chemical coverage and understanding the possible outcomes of chemical exposure on human health.In this webinar, our expert speaker will discuss how a new method with sequential acquisition of targeted and untargeted data can be used to analyze the exposome and the metabolome in a single LC-MS run, providing greater insights into the effects of chemical exposure.Attend this webinar to:<ul><li>Find out about the benefits of sequential targeted and untargeted data acquisition in a single LC-MS run</li><li>Understand how high sensitivity and broad chemical coverage can be achieved simultaneously for performing exposomic and metabolomic experiments</li><li>Discover a novel method that can be tailored for many different applications in the field of small molecule omics</li></ul><blockquote>Presenter: Dr. Vinicius Verri Hernandes (Postdoctoral Researcher at University of Vienna)</blockquote><blockquote>Vinicius obtained his degree in Chemistry followed by a Master in Analytical Chemistry in 2013 from the University of Campinas in Brazil, with focus on mass spectrometry. He later started a joint PhD program between the same university and the Centre for Excellence in Metabolomics in Bioanalysis in Madrid, Spain, working on multiplatform metabolomics on dried blood spots. From 2018 to 2022 he worked as a postdoctoral researcher at the European Research Academy (EURAC) in Bolzano, Italy, being responsible for targeted and untargeted data generation for 5000 samples from the CHRIS populational study. Currently at the University of Vienna, Vinicius focus his work on the combination of targeted and untargeted approaches for exposomics and metabolomics, as well as in the development of analytical workflows for exposure analysis on dried blood spots.</blockquote>

Technology Networks: Bridging Exposomics and Metabolomics in a Single LC-MS Run

Bridging Exposomics and Metabolomics in a Single LC-MS Run

How a new method with sequential acquisition of targeted and untargeted data can be used to analyze the exposome and the metabolome in a single LC-MS run.

Day two: Characterization and discovery<ul><li>Characterize and quantify calreticulin (CALR) arginylation using electron-activated top-down proteomics</li><li>Achieve in-depth profiling of metabolites and lipids in biological samples</li><li>Obtain accurate and reliable metabolite identification using electron-based fragmentation (EAD)</li><li>Detect trace amounts of pesticide residues in food by targeted and non-targeted, IDA and SWATH approaches</li><li>Enhance routine characterization of low-abundant sequence variant (SV) through fast and sensitive EAD-DDA</li></ul><h5>Agenda-at-a-glance</h5>Welcome and introduction to characterization and discoveryTop-down characterization of post-translational arginylation using electron activated dissociation (EAD)<ul><li>Learn about our top-down proteomics workflow for the characterization and quantification of calreticulin (CALR) arginylation. MS1 profile and MS2 fragmentation were characterized by EAD. Preferential fragmentation at the CALR N-terminals yielded sufficient c ions facilitating precise localization of the arginylation sites. Learn about:<ul><li>Arginylation regulates CALR degradation and ER function</li><li>EAD is efficient in characterizing N-terminal arginylation</li><li>The workflow sets up the foundation for unbiased top-down activity-based arginylation profiling</li></ul></li></ul>In-depth metabolomics and lipidomics analyses<ul><li>Routine measurement of metabolites and lipids has become a cornerstone of biomedical research. At the MPC, Helmholtz Munich, non-targeted analysis is based on the SCIEX ZenoTOF 7600 for accurate and in-depth analysis and annotation of metabolites and lipids from different biological specimens.<ul><li>Application of Zeno trap enabled non-targeted workflows to large scale metabolomics and lipidomics studies</li><li>Enhanced sensitivity enables deeper profiling of biological samples</li><li>Increased confidence in identifications through comprehensive structural elucidation using Electron activated dissociation (EAD)</li></ul></li></ul>MetID innovations in pharma: exploring new avenues for metabolite structure elucidationTime-of-flight mass spectrometry applications in food science: targeted and non-targeted approaches<ul><li>Time-of-flight mass spectrometry has become a key tool in analytical laboratories involved in food analyses. This instrumentation can be used for both targeted and non-targeted approaches. In this presentation, we will discuss:<ul><li>Overview of practical targeted and non-targeted approaches in food analysis</li><li>Application of a SWATH® approach to the analysis of pesticide residues in food</li><li>Application of IDA approaches in non-targeted food analyses</li></ul></li></ul>Reduce risk and accelerate cell line development with iCIEF-UV/MS technology<ul><li>Guide decisions during cell line development with the Intabio ZT system with more information on how process changes affect cell line and product stability. &nbsp;<ul><li>How to utilize icIEF-UV/MS to identify sequence variants</li><li>How this information can be used to create a mitigation strategy</li><li>What more information in less time means to groups throughout process development</li></ul></li></ul>Q&amp;A roundtable: A deeper look at high-resolution mass spectrometry<ul><li>Moderated by: ose Castro-Perez, Vice President of Product Management, SCIEX</li><li>Panelists include:<ul><li>Tom Lin, Instructor, Washington University in St. Louis</li><li>Michael Witting, Deputy Head Metabolomics and Proteomics Core and Executive Manager Metabolomics, Helmholtz Munich</li><li>Francisco José Díaz-Galiano, Postdoctoral researcher, University of Almería</li><li>Kirsten Nields, Principal Scientist, J&amp;J Innovative Medicines</li><li>Tatjana Talamantes, Senior Product Manager, Accurate Mass, SCIEX</li></ul></li></ul><blockquote>Moderator: Tatjana Talamantes, Senior Product Manager, Accurate Mass, SCIEXTatjana is a Senior Product Manager at SCIEX, overseeing accurate mass systems since 2021. She collaborates with R&amp;D, sales, and marketing teams to ensure effective project execution and portfolio management.Previously, Tatjana was a Product Manager at MOBILion Systems, leading the pre-commercialization of SLIM-based ion mobility instruments. She also has held roles at Thermo Fisher Scientific as a Sr. Vertical Marketing Specialist and Sr. Field Applications Scientist.Tatjana holds a B.A. in chemistry from Austin College and a Ph.D. in biomedical sciences and biochemistry from the University of North Texas Health Science Center.Jamie holds a B.Sc. in engineering physics from Queen’s University.Presenter: Tom Lin, Instructor, Washington University in St. LouisPresenter: Michael Witting, Deputy Head Metabolomics and Proteomics Core and Executive Manager Metabolomics, Helmholtz MunichPresenter: Francisco José Díaz-Galiano, Postdoctoral researcher, University of AlmeríaPresenter: Kirsten Nields, Principal Scientist, J&amp;J Innovative MedicinesPresenter: Tatjana Talamantes, Senior Product Manager, Accurate Mass, SCIEX</blockquote>

SCIEX summit Day two: Characterization and discovery

Importance of LC-MS in food and environmental testing, pharmaceutical and biopharmaceutical discovery and development and biomedical and omics research.

CIEX summit Day two: Characterization and discovery

Day three: Quantitation and screening<ul><li>Enhanced sensitivity and robustness deliver stringent quantitation for veterinary drug testing for meat</li><li>See how intuitive, compliant-ready SCIEX OS software enables pharmacokinetic parameter monitoring with ease and reliability</li><li>Understand the challenges and best practices for oligoneucleotide analysis by LC-MS&nbsp;</li><li>Discover how exploiting fast acquisition rates can be used to identify and quantify over 2250 fatty-acids lipids</li><li>Hear about the accurate detection and quantitation of trace-lelvel PFAS compounds</li></ul><h5>Agenda-at-a-glance</h5>Welcome and introduction to quantitation and screening&nbsp;&nbsp;&nbsp;&nbsp;Veterinary drug analysis: SCIEX 7500 system vs 7500+ system<ul><li>Biochemie Lab shares their expertise in veterinary drug analysis. With over 25 years of experience and strict adherence to Commission Regulation (EU) No 37/2010, Biochemie Lab processes more than 100,000 samples annually, providing comprehensive food and environmental testing.<ul><li>Learn how Biochemie Lab conducts veterinary drug testing with specialized veterinarians, covering a wide range of analyses, including residual veterinary drugs, anabolic substances, and microbiological tests.&nbsp;</li><li>Discover how they overcome challenges in analyzing complex animal-origin matrices like meat and offal using the SCIEX QTRAP 7500 system.</li><li>Explore their proficiency testing, method validation results, and ask questions directly from leading experts in the field.</li></ul></li></ul>Maximizing analytical potential and navigating changes in the validated laboratory with SCIEX OS software<ul><li>Having the right information available at every stage of the process is vital to bringing safe and effective therapies to market.. SCIEX OS software is a vital component of this process, from discovery to development. See how:<ul><li>Your pharma lab workflows can benefit from SCIEX OS software</li><li>Central Admin Console enables comprehensive audit configurations for full traceability</li><li>Professional services are available to assist in migrating from legacy Analyst software and change control support plansis</li></ul></li></ul>Approaches for the bioanalytical analysis of oligonucleotide therapies<ul><li>Oligonucleotide therapeutics are on the rise in drug development and regulatory submissions. These drugs face challenges with bioanalytical extraction and analytical detection due to their chemical backbone or other stability-enhancing modifications.<ul><li>Learn about bioanalytical challenges and best practices for oligonucleotide analysis</li><li>Hear case studies in the quantitation of oligonucleotide therapies using different mass spectrometry platforms</li><li>Gain insights into improved method development for obtaining validated assays for regulatory evaluations using high-resolution mass spectrometry in early-stage development</li></ul></li></ul>Fast scanning quantitative lipidomics analysis using the SCIEX 7500+ system<ul><li>A panel of &gt;2250 lipids was used to demonstrate the power and capability of the SCIEX 7500+ system to sensitively identify and quantify lipids at the fatty acid level using a multiple reaction monitoring (MRM). HILIC-like chromatography provides class separation to mitigate inter-lipid class isobaric overlap, but means that the speed at which individual MRM transitions are measured is crucial to ensure good coverage and quantitative accuracy.<ul><li>The ~4X faster analytical speed of the SCIEX 7500+ system improves the quantitative performance of a large, broadly targeted lipid panel</li><li>The number of lipid molecular species quantified with %CV &lt; 20 increased 59% during a period of the highest</li><li>MRM concurrency (n = 925) compared to the fastest speed recommended on the SCIEX 7500 system The faster MRM acquisition rates improve peak shapes by increasing the number of data points across the peak and providing better resolution of near-eluting lipid isomers</li></ul></li></ul>From sample collection to data processing - PFAS program at State Hygienic Lab<ul><li>The State Hygienic Lab at University of Iowa had the PFAS program running for couple of years and is accredited and certified by the state, EPA, and UCMR5 program to test for PFAS in water samples. However, testing encompasses different environmental and biological matrices. This presentation will look at the program and focus on:<ul><li>Approaches from sample collection to data processing and reporting.</li><li>Testing for PFAS in water matrices (drinking, raw, well, surface, and groundwater) based on EPA 537.1 and 533 FAS methods.</li><li>New method for PFAS in biological samples.</li></ul></li></ul>Q&amp;A roundtable: &nbsp;quantitation and screening<ul><li>Moderated by: Ian Moore, Sr. Technical Product Manager, Nominal Mass, SCIEX</li><li>Panelists include:<ul><li>Roberto Riccio, Biochemie Lab</li><li>Shane Karnik, Senior Laboratory Director, Aliri Bioanalysis</li><li>Ebru Selen, Biologics Applications Scientist, SCIEX</li><li>Paul Baker, Senior Scientific Liason, Lipidomics and Metabolomics, SCIEX</li><li>Craig Butt, Senior Manager, Scientific Marketing, Applied Markets, SCIEX</li></ul></li></ul><blockquote>Moderator: Ian Moore, Sr. Technical Product Manager, Nominal Mass, SCIEXWith over ten years in product development, Ian is the Senior Technical Product Manager for nominal mass LC-MS/MS systems at SCIEX. He has also served as a Technical Product Manager and Global Technical Marketing Manager. Ian began his SCIEX career as an Application Scientist, focusing on biologics bioanalysis and DiscoveryQuant software validation.Before SCIEX, Ian was the Lead Analytical Scientist at Custom Biologics, overseeing LC-MS/MS method development and clinical trial analysis. He also served as a Senior Scientist at Affinium Pharmaceuticals, focusing on metabolic stability profiling and enzyme inhibition assays.Ian holds a postdoctoral position at McMaster University, specializing in antibiotic resistance and enzyme inhibitor screeningPresenter: Roberto Riccio (Biochemie Lab)Presenter: Shane Karnik (Senior Laboratory Director, Aliri Bioanalysis)Presenter: Ebru Selen (Biologics Applications Scientist, SCIEX)Presenter: Paul Baker (Senior Scientific Liason, Lipidomics and Metabolomics, SCIEX)Presenter: Craig Butt (Senior Manager, Scientific Marketing, Applied Markets, SCIEX)</blockquote>

SCIEX summit Day three: Quantitation and screening

Food allergies are a public health and regulatory challenge, with an estimated 1–2% of adults affected by food allergies. Risk analysis and management of allergens within the food and beverage industry rely on accurate allergen analysis.High-performance liquid chromatography high-resolution mass spectrometry (HPLC-HRMS) could be the future of food allergen analysis.In this webinar, our expert speaker will discuss how HPLC-HRMS can detect a wide range of allergens in a single run, reducing the time and effort involved in food analysis. He’ll also highlight how integrating HPLC with HRMS approaches enhances accuracy and makes allergen detection more reliable, ensuring robust food safety and compliance with regulatory standards.<h4>Attend this webinar to:</h4><ul><li>Learn how to multiplex allergen detection &nbsp;</li><li>Improve the accuracy and speed of your food analysis &nbsp;</li><li>Discover a complete workflow including sample preparation and data analysis</li></ul><blockquote>Presenter: Prof. Jens Brockmeyer (Head of Department, Food Chemistry, University of Stuttgart, Germany)</blockquote>

Technology Networks: Moving Towards the Next Generation of Food Allergen Analysis

Moving Towards the Next Generation of Food Allergen Analysis

How HPLC-HRMS can detect a wide range of allergens in a single run, reducing the time and effort involved in food analysis.

Clinical blood analysis is crucial for monitoring health and diagnosing diseases, with blood-based biomarkers playing a key role.However, current detection methods often lack sufficient coverage. Mass spectrometry-based proteomics provides a robust solution for in-depth plasma proteome analysis, but precise sample preparation is essential.This webinar will guide you on maximizing plasma proteome coverage and optimizing sample preparation, whether using plasma or serum. Dr. König and Dr. Wendt will discuss developing an optimized, automated workflow for comprehensive plasma biomarker discovery, showcasing results from two complementary techniques: LC-MS and Olink.<h4>Attend this webinar to:</h4><ul><li>Discover how to efficiently prepare blood-derived samples, including plasma and serum</li><li>Explore how to implement a fully automatable, reproducible and standardized plasma workflow with scalable throughput</li><li>Achieve comprehensive plasma proteome characterization, addressing the dynamic range challenge for deeper insights</li><li>Learn to apply LC-MS-based proteomics combined with affinity-based methods to discover novel disease biomarkers</li></ul><blockquote>Presenter: Dr. Ann-Christine König (Proteomics Core Facility Manager, Helmholtz Zentrum Munich) Presenter:&nbsp;Dr. Fabian Wendt (Product and Application Manager, Mass Spectrometry, Tecan)</blockquote>

Technology Networks: Unlocking the Plasma Proteome: Advanced Profiling and Biomarker Discovery

Unlocking the Plasma Proteome: Advanced Profiling and Biomarker Discovery

Maximizing plasma proteome coverage and optimizing sample preparation, whether using plasma or serum.

Unlocking the Plasma Proteome: Advanced Profiling

Join us as we introduce our path to visualize molecules from tissue at single cell resolution using DESI MS imaging, with the commercial DESI XS ionization source coupled to Xevo G3 QToF Mass Spectrometer.This webinar will explain how to easily transition to high resolution MS Imaging with a traditional entry level commercial DESI MS imaging toolkit.<h4>Learn how to:</h4><ul><li>Understand High spatial resolution MS Imaging is now accessible to all labs and applications</li><li>Access single cell DESI Imaging with the combination of DESI XS and Xevo G3 QToF</li><li>Leverage both high sensitivity and high speed of acquisition with the Xevo G3 QToF without compromising MS Imaging data quality</li><li>Utilize HDI 1.8 Imaging software for microscope mode analysis for effective use of time in MS Imaging experiments</li><li>Obtain comprehensive and detailed spatial information with limited sample preparationAdd MSI analysis into a multi-modal imaging workflow with ease</li></ul><blockquote>Presenter:&nbsp;Dr Jamie Reilly (Postdoctoral Researcher, University of Galway)Dr. Jamie Reilly is a postdoctoral researcher in NUIG Galway. Prior to joining the CELLIMAGE project, Jamie undertook his PhD in Regenerative Medicine in REMEDI, where he used bioinformatics to analyze molecular pathways in cellular and animal models of autism spectrum disorder (ASD). Jamie attended Trinity College Dublin (TCD) for his undergraduate degree in Genetics, and has a Masters in Biotechnology from Queens University Belfast.Presenter:&nbsp;Dr. Mark Towers (Principal Scientist - MS Technology, Waters)Mark Towers gained his PhD from the University of Reading in Bioanalytical chemistry on the Development of applications and techniques for UV-Liquid-MALDI-MS. Mark joined Waters over 10 years ago into the Scientific operations team as a senior scientist, working on high resolution mass spectrometry and imaging.Mark’s primary area of focus has been surface analysis by desorption electrospray ionisation (DESI) with over 7 years experience and matrix assisted laser desorption ionisation for over 14 years, principally but not limited to tissue sections for the detection and distribution mapping of a wide range of molecules.Presenter: Dr. Joanne Ballantyne (Director, MS Imaging program, Waters Corporation)Joanne completed a PhD in Mass Spectrometry at UMIST in Manchester 2002, in collaboration with UK Ministry of Defence's Science and Technology Lab (Dstl). This was followed by a post-doc at NIH in Bethesda, USA, working in OMICS for the NIMH. After returning to the UK, and time as a MALDI applications chemist at Shimadzu Biotech, Joanne joined Waters Corporation in 2007 as a member of the OMICS Application team in Manchester and progressed to managing the team. Following this Joanne spent a number of years in Business Development and Field Marketing for discovery applications in the Northern European region. At the end of 2018 Joanne joined the Product Management group with responsibility for the SYNAPT and MS Imaging technologies. After gaining ILM7 accreditation in strategic leadership, Joanne is now Director of the MS Imaging program.</blockquote>

Waters Corporation: Towards Single Cell Imaging Session 1

Towards Single Cell Imaging Session 1

How to easily transition to high resolution MS Imaging with a traditional entry level commercial DESI MS imaging toolkit.

This session will provide a comprehensive introduction to the user interface, ensuring you can navigate with ease. Discover the various acquisition modes available and learn how to select the best one for your specific application.Additionally, we will explore the innovative Intelligent Reflex feature, highlighting its benefits in boosting your productivity.Whether you’re new to MassHunter or looking to refine your skills, this webinar is designed to enhance your understanding and efficiency.<blockquote>Presenter: Christian Hegmanns (Application Specialist LC/MS, Agilent Technologies, Waldbronn, Germany)Christian Hegmanns is a state-certified food chemist and works at Agilent as an LC/MS application specialist.With over 10 years of experience in the field of instrumental analysis, Christian develops customer-oriented solutions for a variety of applications with a focus on food analysis.</blockquote>

Agilent Technologies: MassHunter Masterclass Months

MassHunter Acquisition Q-TOF Part I – Basic Overview

Join us for an insightful webinar where we delve into the essentials of MassHunter Acquisition Q-TOF. 

This webinar will guide you through optimizing your Q-TOF for superior data quality by selecting the most suitable tune mode for your samples.We will delve into various MS acquisition modes, including MS only, All Ions (QRAI), Auto MS/MS (directed MS/MS; targeted MS/MS), and PRM mode.Learn how to fine-tune method settings to enhance your data quality and achieve the best analytical results. Whether you’re a seasoned user or new to QTOF, this session will provide valuable insights to elevate your mass spectrometry.<blockquote>Presenter: &nbsp;Stefan Schaebler (Application Specialist LC/MS, Agilent Technologies)Stefan completed his PhD in Biology, specializing in LC-MS-based lipidomics and metabolomics. Following his doctoral studies, he joined Agilent Technologies as an LC/MS Application Specialist. In this role, Stefan focuses on small molecule applications using LC-QTOF, with a strong emphasis on software tools and data interpretation.</blockquote>

MassHunter Acquisition Q-TOF Part II – Advance Settings

Join us for an in-depth exploration of advanced settings in MassHunter Acquisition for Q-TOF systems.

<div><div>Therapeutic synthetic oligonucleotides represent unique analytical challenges in late-stage development. To meet the stringent regulatory requirements, highly specific and sensitive methods such as liquid chromatography-mass spectrometry (LC/MS) must be used. However, neither chromatography nor mass spectrometry data systems have the capabilities, both in function and in data integrity, for the typical QC analyst end user to run a highly complex method such as purity, assay, and impurity profiling for therapeutic oligos such as anti-sense oligonucleotides.In this presentation, we present a paradigm shift in software with Oligo Analysis Accelerator for OpenLab CDS. This application streamlines the analytical workflow by using a fit-for-purpose user interface while leveraging existing data integrity and compliance architecture within OpenLab CDS.<h4>By attending this webinar, you will:</h4><ul><li>Understand the fundamentals of ion-pair reversed-phase LC/MS for oligonucleotides</li><li>Discover how a single quadrupole detector is used for impurity profiling of anti-sense oligonucleotides</li><li>Learn how fit-for-purpose software for LC/MS analysis in QC lot release can save time and enhance quality</li></ul><h5>Who should attend</h5><ul><li>Analytical chemists interested in cutting-edge software for large molecule late-stage development</li><li>Analytical research and development labs interested in developing robust methods for single-stranded oligo therapeutics</li><li>Process scientists who rely on in-process control purity results to optimize synthesis and purification for oligos</li><li>Quality assurance and quality control personnel supporting oligo testing labs</li></ul><blockquote>Presenter: Brian Rivera (Software Product Manager, Agilent Technologies)Brian Rivera is a software product manager at Agilent Technologies with 20 years of experience in HPLC analysis of large molecules.</blockquote></div></div>

Separation Sciences: Boost Efficiency in Oligonucleotide QC with Software Designed for the Job

Boost Efficiency in Oligonucleotide QC with Software Designed for the Job

In this presentation, we present a paradigm shift in software with Oligo Analysis Accelerator for OpenLab CDS.

Oligonucleotide QC with Software Designed for the Job

<div><div><div>MALDI MS is ideally suited to increase productivity with rapid automated measurements. They provide near instant mass verification and information about impurities and degradants, which is valuable in quality control, assay optimization, and verification of substrates. Learn how the novel neofleX™ MALDI-TOF/TOF system&nbsp;enhances these workflows.</div></div></div><div><div><div><h5>Key Learning Objectives:</h5><ul><li>Overview of neofleX™ technology and its benefits to life sciences applications</li><li>Rapid automated analysis of a wide range of analytes including oligonucleotides and peptides</li><li>Software solutions for batch mode post-processing of automated runs</li></ul></div></div></div><div><div><div><h5>Who Should Attend:</h5><ul><li>Characterization team leaders in biopharma companies and CROs</li><li>Mass spectrometry core lab managers</li><li>Anyone who is interested in rapid automated MS analysis</li><li>Researchers who would like to learn about the latest MALDI-TOF/TOF technology</li><li>Anyone who is interested in oligonucleotide and peptide analysis</li></ul><div><div><div><div><blockquote><div>Presenter: Sergei Dikler, Ph.D. (Senior Market Manager, MALDI Technologies, Bruker Scientific LLC, Billerica, MA, USA)Sergei Dikler, Ph.D., is a Senior Market Manager focused on promoting MALDI technologies. Dr. Dikler received his Ph.D. degree at Texas A&amp;M University. He is an expert in MALDI application development and high-throughput MSPresenter: Sinduri Vuppala, Ph.D. (Field Applications Specialist, Bruker Scientific LLC, Billerica, MA, USA)Sinduri Vuppala, Ph.D., is a Field Applications Specialist for non-imaging MALDI applications at Bruker. Dr. Vuppala received her Ph.D., in Analytical Chemistry at the University of South Florida with focus on method development involving MALDI and CCS technologies.</div></blockquote></div></div></div></div></div></div></div>

Bruker: Rapid automated analysis using the novel neofleX™ platform

Rapid automated analysis using the novel neofleX™ platform

MALDI MS is ideally suited to increase productivity with rapid automated measurements. 

LCMS webinars focusing on LC/TOF - page 11