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

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

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

Webinars LabRulezLCMS Week 07/2026

Charge detection mass spectrometry (CDMS) allows direct mass determination of individual ions and is increasingly used to study heterogeneous biological samples. This work demonstrates the use of Orbitrap-based CDMS/Direct Mass Technology (DMT) for quantitative analysis of transthyretin (TTR) tetramer samples below 100 kDa, extending CDMS beyond its traditional qualitative role.DMT resolved wild-type and C-terminally modified TTR homotetramers, as well as hybrid tetramers, enabling kinetic analysis of subunit exchange and stability. The approach also quantified thyroxine binding to TTR variants, revealing differences in binding affinity linked to C-terminal modification. By separating overlapping m/z signals through charge measurement, CDMS enables accurate mass and abundance determination, highlighting its potential for quantitative analysis of complex protein systems.<blockquote><h4>The original article</h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771">Dissecting Heterogeneous Populations of Protein-Complex Samples Using Direct Mass Technology</a></h4>Robert L. Rider, Jared Hampton, Zhenyu Xi, Carter Lantz, Sangho D. Yun, Weijing Liu, Rosa Viner, Arthur Laganowsky, and David H. Russell*Anal. Chem. 2025, 97, 49, 27057–27063<a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.analchem.5c05771">https://doi.org/10.1021/acs.analchem.5c05771</a><h6>licensed under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/">CC-BY 4.0</a></h6></blockquote>Selected sections from the article follow. Formats and hyperlinks were adapted from the original.Transthyretin (TTR) is a homotetrameric transport protein that circulates in plasma and cerebrospinal fluid, delivering thyroxine (T4) and retinol-binding protein–vitamin A complexes. <a href="javascript:void(0);">(1)</a> The stability of the TTR tetramer is central to its physiological role because dissociation into monomers can initiate misfolding and amyloid formation, leading to systemic or hereditary transthyretin amyloidosis. <a href="javascript:void(0);">(2)</a> Subunit exchange between wild-type (WT) and variant TTR proteoforms, including disease-associated mutations such as V30M and V122I, have been implicated in amyloid progression by generating hybrid tetramers (tetramers containing WT and mutant subunits) with altered stabilities. <a href="javascript:void(0);">(3,4)</a> Ligand binding, particularly at the two thyroxine-binding sites located at the dimer–dimer interface, can kinetically stabilize the tetramer and modulate amyloidogenicity. <a href="javascript:void(0);">(5,6)</a> Accurate measurement of both subunit exchange kinetics and ligand binding stoichiometry is therefore critical for elucidating the TTR dynamics and stability.Affinity or sequence tags are widely employed in protein expression, purification, or detection. <a href="javascript:void(0);">(7,8)</a> While these tags are often assumed to be inert, their influence on protein structure and dynamics are rarely examined in detail. <a href="javascript:void(0);">(9,10)</a> Protein tags at the N- and C-terminus of TTR have been shown to have differing gas phase stabilities from those of WT-TTR. <a href="javascript:void(0);">(11)</a> The C-terminus is of particular interest because this region participates in the dimer–dimer interface that governs tetramer stability. <a href="javascript:void(0);">(11,12)</a> Characterizing how the C-terminal tag (CT) (-ASGENLFYQ) affects TTR’s solution stability and ligand binding is not only relevant for understanding TTR dynamics but also provides an example of how expression tags can alter protein dynamics. <a href="javascript:void(0);">(13)</a>Native mass spectrometry (nMS) has been invaluable for characterizing protein complexes, <a href="javascript:void(0);">(14)</a> yet conventional nMS often struggles with heterogeneous samples where overlapping charge state distributions and adduct heterogeneity limit resolution and quantitation. <a href="javascript:void(0);">(15)</a> Charge detection mass spectrometry (CDMS) addresses these limitations by independently measuring the charge and m/z of individual ions, enabling the direct determination of molecular mass and abundance. Development of CDMS has largely focused on achieving higher mass resolution <a href="javascript:void(0);">(16)</a> and extending measurements toward assemblies into the GDa range. <a href="javascript:void(0);">(17,18)</a> However, there is untapped utility for CDMS experiments other than mass and proteoform determination. Jordan et al. showed the capability to assess conformational heterogeneity of mAb aggregates using the added charge dimension that CDMS provides. <a href="javascript:void(0);">(19)</a> The current work demonstrates that CDMS can separate proteoforms with overlapping m/z values based on charge and quantify their relative abundances in complex mixtures. While nMS is already a highly quantitative technique, our results establish CDMS as an equally powerful tool for quantitative analysis in heterogeneous systems. <a href="javascript:void(0);">(20,21)</a>Here, we apply Orbitrap-based CDMS/Direct Mass Technology (DMT) using the selective temporal overview of resonant ions (STORI) approach <a href="javascript:void(0);">(22,23)</a> to quantitatively compare WT-TTR and CT-TTR, focusing on two biologically relevant properties: tetramer stability assessed via subunit exchange kinetics and ligand-binding affinity. Conventional nMS cannot fully resolve the overlapping charge states of WT- and CT-TTR or their ligand-bound states. However, DMT can resolve these species by directly measuring the mass (m/z × charge), enabling quantitation of all proteoforms. The data reveal that the CT tag alters tetramer stability and thyroxine-binding affinity, demonstrating the structural sensitivity of TTR to modifications at its C-terminus. More broadly, this work demonstrates the impact that protein tags can have on native protein interactions and highlights the broader utility of quantitative CDMS for probing heterogeneous biological samples.<h4>Experimental Section</h4><h5>Data Collection</h5>All experiments were conducted on a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/560">Thermo Scientific Q-Exactive UHMR</a> with added DMT capabilities (Bremen, Germany). Before DMT, mass spectra were collected at various resolving powers (6–200k) for each sample, with the instrument parameters reported in the Supporting Information (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Table S1</a>). For DMT experiments, the trapping gas pressure in the HCD cell was reduced to 0.3–0.8 to attenuate the signal intensity to a single ion level, as well as decreasing the UHV pressure to assist ion retention through the entire transient of Orbitrap analysis. We observed no significant difference between mass spectra collected at various HCD cell pressures (Supporting Information, <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figure S1</a>). For DMT collection, automated ion control (AIC) and 100% target density were used with 200k resolving power.<h4>Results and Discussion</h4>CDMS has emerged as a powerful tool for analyzing heterogeneous biomolecular samples, enabling accurate, direct mass determination by simultaneously measuring the charge and m/z for individual ions. While CDMS has been widely applied for qualitative analyses, its potential for quantitative and less than MDa applications remains underexplored. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>A shows the theoretical mass spectrum of WT-TTR (14+ to 16+) and CT-TTR (15+ to 17+) homotetramers, where the two proteoforms become increasingly resolved as the charge states increase (&lt;3900 m/z). <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>B zooms in on the 14+ (WT) and 15+ (CT) charge states, highlighting their strong overlap, which prevents accurate deconvolution of the proteoforms by conventional methods. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>C displays theoretical distributions for 0, 1, and 2 T4 bound states of both WT- and CT-TTR tetramers, where &lt;3900 m/z has observable separation between all proteoforms. However, for the 14+ and 15+ charge states of WT- and CT-TTR, respectively, the 0 T4- and 1 T4-bound populations overlap (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>D). Furthermore, commonly adducted species (Na+, K+, and Zn2+) observed in experimental spectra broaden these distributions, making it increasingly difficult to distinguish and deconvolute the proteoforms (see <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figure S2</a>). Here, we employ Orbitrap-based CDMS/DMT to overcome this m/z overlap to resolve and quantify hybrid tetramer formation and T4 binding.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Anal_Chem_2025_97_49_27057_27063_Figure_1_A_Theoretical_mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_47232849d9.jpg" alt="Anal. Chem. 2025, 97, 49, 27057–27063: Figure 1. (A) Theoretical mass spectra of WT-TTR and CT-TTR homotetramers. (B) Zoomed-in view of the 14+ WT-TTR and 15+ CT-TTR distributions to show the large overlap of the proteoforms. (C) Theoretical mass spectra of WT-TTR and CT-TTR homotetramers with thyroxine (T4) binding. (D) Zoomed-in view of the 14+ WT-TTR and 15+ CT-TTR distributions where the 0 and 1 T4 have overlapping distributions. These theoretical distributions do not contain any commonly adducted species (Na+, K+, Zn2+), which broaden the distributions and create more overlap even for the proteoforms in the range 3300–3900 m/z (see Figure S2)." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Anal_Chem_2025_97_49_27057_27063_Figure_1_A_Theoretical_mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_47232849d9.jpg 187w," sizes="100vw" width="1417" height="1182"><h5>Thyroxine Binding to TTR Homotetramers</h5>Thyroxine is the less active form of a thyroid hormone important for metabolism that binds to TTR for transport throughout plasma and cerebral spinal fluid. <a href="javascript:void(0);">(31)</a> Turnover of T4 into T3 (active) occurs after dissociation, where it can then modulate gene expression via binding to nuclear receptors. <a href="javascript:void(0);">(32)</a> The TTR tetramer gains substantial stability as it binds up to 2 T4 at the tetramer interface, decreasing tetramer dissociation and SUE. <a href="javascript:void(0);">(33)</a> This has been shown previously to decrease the amyloidogenic rate of TTR, which led to tafamidis (similar in structure to T4) to be designed and is currently the only drug that is approved for clinical treatment of TTR amyloidosis. <a href="javascript:void(0);">(34)</a> Measuring the difference in binding affinity between TTR proteoforms may provide insight into regions of TTR or TTR intermolecular/intramolecular interactions that are important for binding of small molecules such as tafamidis and T4.DMT was further applied to quantify T4 binding to WT- and CT-TTR homotetramers, highlighting the technique’s utility in probing protein–ligand interactions. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig3">Figure 3</a>A shows a representative mass spectrum of TTR homotetramers in the presence of T4. While ligand-bound species can be observed, homotetramers cannot be confidently resolved across the entire 3000–5000 m/z range. By leveraging the charge-resolving capabilities of DMT, we achieve separation of the homotetramers (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig3">Figure 3</a>B,C) and the 0, 1, and 2 ligand-bound states. The 2D plot clearly shows the gain in resolution achieved when charge is simultaneously measured with m/z by separating the 14+ and 15+ charge states for WT and CT, respectively, in the range 3900–4200 m/z. Additionally, using ion mobility does not provide the same kind of 2D resolution due to the similarity in arrival times for the homotetramer proteoforms, as evidenced by <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figures S4 and S5</a> (see the Supporting Information). These data provide evidence that when ion mobility is able to separate out species that overlap in m/z yet differ in mobility, CDMS could be an alternative or used complementarily since the species likely also differ in charge.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Anal_Chem_2025_97_49_27057_27063_Figure_3_A_Mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_with_thyroxine_binding_61b1e98a94.jpg" alt="Anal. Chem. 2025, 97, 49, 27057–27063: Figure 3. (A) Mass spectra of WT-TTR and CT-TTR homotetramers with thyroxine binding. Ligand binding can be resolved, but homotetramers cannot be confidently identified. Charge states labeled are for WT; CT is always one charge state higher at the same m/z range. (B) DMT heatmap resolving WT-TTR and CT-TTR homotetramers with the additional measurement of charge. (C) Deconvoluted mass spectrum from DMT analysis. Both homotetramers and their ligand binding are resolved, and fit for analysis is shown in red. (D) Mole fraction of each homotetramer and their thyroxine binding species. Error bars represent the standard deviation of replicates (n = 3). The significance for each ligand state is in respect to the left adjacent state. *p &lt; 0.05." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Anal_Chem_2025_97_49_27057_27063_Figure_3_A_Mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_with_thyroxine_binding_61b1e98a94.jpg 181w," sizes="100vw" width="1266" height="1094"><h4>Conclusion</h4>This work demonstrates that quantitatively, Orbitrap-based CDMS/DMT can determine differences in protein-complex stability and ligand binding. By directly comparing WT- with CT-TTR, we show that the CT tag accelerates tetramer dissociation while enhancing T4 binding affinity. These results indicate that the C-terminus, located at the dimer–dimer interface, plays a more significant role in TTR stability and ligand recognition than previously appreciated. <a href="javascript:void(0);">(12)</a> Even the addition of a short peptide sequence perturbs noncovalent interactions at the interface, likely altering solvent accessibility, and the dynamics of the thyroxine binding channel. <a href="javascript:void(0);">(37,54)</a> Such findings underscore the importance of evaluating how seemingly minor sequence modifications, such as affinity tags, can influence fundamental biophysical properties.Beyond TTR, this work positions quantitative CDMS as a broadly applicable strategy for analyzing heterogeneous protein systems, where charge domain separation overcomes the resolution limits of m/z domain measurements in traditional nMS experiments. While much of the field has emphasized extending CDMS to ultrahigh masses and maximal resolution, <a href="javascript:void(0);">(16,18)</a> our results highlight the underexplored potential of applying the method in the 1000–10,000 m/z range common to nMS experiments. This capability is directly relevant to heterogeneous membrane protein complexes, which often display broad distributions of oligomeric states, PTMs, lipid, and ligand adducts that complicate spectra. <a href="javascript:void(0);">(48,55)</a> Similarly, mAbs can oligomerize and exhibit mass heterogeneity from variable glycosylation, affecting pharmacokinetics, effector function, and stability. <a href="javascript:void(0);">(19)</a> CDMS may resolve and quantify such proteoforms in a single experiment without the need for charge reduction or chemical derivatization. <a href="javascript:void(0);">(48,56,57)</a>

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

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

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Waters Corporation

This online event has been designed for our customers and brings together opinion leaders, top scientists and industry innovators to share their research in the biopharma field.
The technologies presented will be CE and LC-MS.
Agenda:
<h5>10:00–10:10 Welcome and introduction</h5>
<ul>
<li>Steve Lock, SCIEX</li>
</ul>
<h5>10:10–10:35 Use of LC-MS in process analytical testing as part of development of a continuous manufacturing workflow</h5>
<ul>
<li>Daniel Myatt / Ronan Gough, CPI</li>
</ul>
<h5>10:35–11:00 Tips and tricks for biotherapeutics characterization by peptide mapping</h5>
<ul>
<li>Giulia Calloni, SCIEX</li>
</ul>
<h5>11:00–11:25 Developing methods for SEC-MS and IEX-MS for the analysis of biotherapeutics</h5>
<ul>
<li>Sarah Nguyen, Strasbourg University</li>
</ul>
<h5>11:25–11:35 Break</h5>
<h5>11:35–12:00 The power of CZE analysis for characterization of NANOBODY® molecules</h5>
<ul>
<li>Dries Dejaegere, Sanofi</li>
</ul>
<h5>12:00–12:25 Multi-capillary gel electrophoresis to increase throughput for the purity analysis of biotherapeutic proteins</h5>
<ul>
<li>Theresa Merlino, The Janssen Pharmaceutical Companies of Johnson &amp; Johnson</li>
</ul>
<h5>12:25–12:50 A disruptive approach to the characterization of mAb charge variants during biopharmaceutical process development</h5>
<ul>
<li>Greg Adams, FUJIFILM</li>
</ul>
<h5>12:50–13:00 Wrap-up and Q&amp;A</h5>
<blockquote>
Presenter: Steve Lock, PhD (Snr. Marketing and Market Development Manager, Biopharma, EMEAI, SCIEX)
</blockquote>
<blockquote>
Steve obtained his PhD in Physical Organic Chemistry from the University College of Swansea in 1993 and is a chartered chemist and a member of the Royal Society of Chemistry. He has worked for SCIEX in various technical roles for over 20 years and has presented at over 80 international meetings around the world. He currently works closely with customers in the biopharmaceutical industry. Steve is also currently an Adjunct Professor at the University of Pannonia.
</blockquote>
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/SCIEX_agenda_day_1_6818ee0331/SCIEX-agenda-day-1.jpg" alt="SCIEX - agenda day 1.jpg"/>

SCIEX: SCIEX Biopharma meeting - 3rd edition! Day 1 - Gene therapy, vaccines and oligonucleotides

SCIEX Biopharma meeting (Day 1) - Gene therapy, vaccines and oligonucleotides

Gene therapy, vaccines and oligonucleotides. The technologies presented will be CE and LC-MS.

Day 1 - Gene therapy, vaccines and oligonucleotides

Welcome to The Analytical Scientist’s Trends and Challenges in PFAS Analysis forum!
Per- and poly-fluorinated alkyl substances, or PFAS, are a family of synthetic substances used in everyday products, such as stain and grease-repellent coatings and have appeared in almost all foods and drinking water. Toxic at extremely low levels, regulators demand low detection limits, and the list of PFAS compounds under investigation continues to expand. 
We recently asked our readers for their thoughts on the challenges involved in PFAS analysis, whether current methods are up to the task, and what analytical advances may be on the horizon. 
Here, our panel of experts will discuss the survey findings and share their perspectives on the latest trends and best practices in PFAS analysis. 
The event will have three parts: 
<ul>
<li>Part I: A discussion of the results of our recent vendor-neutral audience survey (10-15 minutes).
</li>
<li>Part II: Technology/application-focused presentations from each of our speakers (15 minutes each).
</li>
<li>Part III: A chance for you to ask our speakers questions as part of an audience Q&amp;A (15 minutes).
</li>
</ul>
<blockquote>
Presenter: Day Powell (Environmental Application Specialist , Agilent)
</blockquote>
<blockquote>
Day has worked for Agilent as an Environmental Specialist for one year. Before this he worked for a major UK Water company (United Utilities) as a senior analyst responsible for developing new methodologies for both LC/MS and GC/MS applications.
</blockquote>
<blockquote>
Day has analysed PFAS for several years and helped United Utilities to gain UKAS accreditation for determining 47 PFAS by LC/MS in drinking water using direct injection to address the latest Drinking Water Inspectorate (DWI).
</blockquote>
<blockquote>
Presenter: Marcus Chadha (EMEA Applications Specialist Manager, Agilent) Dr. Marcus Chadha has worked for Agilent for seven years where he first worked as an LC/MS Field Application Specialist before moving on to being the EMEA Applications Specialist Manager in 2021.
</blockquote>
<blockquote>
In his roles he has collaborated with our Environmental and Food customers, developed new methods, and trained LC/TQ and LC-Q/TOF MS workflows to new and existing customers.
</blockquote>
<blockquote>
He now coordinates these activities using his team of GC/MS and LC/MS application specialists. Marcus is also responsible for the market specialisation activities for the environmental market across Europe.
</blockquote>
<blockquote>
Presenter: Linx Waclaski (Product Manager for Ion Chromatography, Metrohm USA)
</blockquote>
<blockquote>
Linx Waclaski is the Product Manager for Ion Chromatography at Metrohm USA, in Riverview, Florida. He has years of experience in multiple chromatographic techniques, including ion chromatography, gas chromatography, liquid chromatography, and mass spectrometry, with extensive experience in R&amp;D and applications development.
</blockquote>
<blockquote>
His chromatography applications experience extends across environmental, food safety, and life sciences industries. He has an M.S. in Forensic Science from Duquesne University.
</blockquote>
<blockquote>
Presenter: Ruth Marfil-Vega (Senior Market Manager - Environmental, Shimadzu)
</blockquote>
<blockquote>
Dr. Ruth Marfil-Vega has 20 years of expertise in environmental chemistry and engineering in the US and Europe. She has worked with the EPA and the utilities industry to design and execute comprehensive solutions for addressing new environmental and water quality issues, including PFAS, regulated and unregulated DBPs, and other emerging contaminants.
</blockquote>
<blockquote>
Since Ruth joined Shimadzu five years ago, she has continued to work with environmental stakeholders to ensure that analytical instrumentation and workflows support their success.
</blockquote>
<blockquote>
She earned a BSc in Chemistry from the University of Valladolid (Spain) and a PhD in Environmental Science and Engineering from the University of Cincinnati.
</blockquote>

Agilent Technologies: Trends and Challenges in PFAS Analysis

Trends and Challenges in PFAS Analysis

Survey findings and perspectives on the latest trends and best practices in PFAS analysis.

Glycosylation plays a crucial role in determining the pharmacological properties of biotherapeutics. The molecular heterogeneity of glycosylated biotherapeutics makes it difficult to provide thorough characterization of intact glycoproteins by mass spectrometry.
Current methods for analyzing biotherapeutics only measure fragments of the compound or rely on partial digestion of the glycans to reduce sample complexity. These limitations pose important risks and challenges for biotechnology companies that need to report human-compatible and consistent glycosylation, critical for drug safety and efficacy. 
We will present a new approach to glycoform fingerprinting that uses proton-transfer charge-reduction with gas-phase fractionation to analyze intact glycoproteins by mass spectrometry. The method provides a detailed landscape of the intact molecular weights present in biotherapeutic protein preparations in a single experiment and offers insights into glycoform composition when coupled with a suitable bioinformatic strategy. In addition, we highlight the application of charge detection native mass spectrometry (Direct Mass Technology mode) towards the elucidation of masses and aggregation of heterogeneous glycosylated biotherapeutics. 
Key Learning Objectives:
<ul>
<li>How to elucidate masses from heterogeneous glycosylated biotherapeutics 
</li>
<li>Learn how proton transfer charge reduction (PTCR) can simplify complex protein mixtures 
</li>
<li>Learn when to use PTCR based methods compared to Direct Mass Technology mode for analysis of biotherapeutics
</li>
</ul>
Who Should Attend:
<ul>
<li>Laboratory Managers 
</li>
<li>Biopharmaceutical Researchers 
</li>
<li>Protein Scientists
</li>
</ul>
<blockquote>
Presenter: Wendy Sandoval (Director, Translational Mass Spectrometry, Genentech)
</blockquote>
<blockquote>
Presenter: Ann Thayer (Contributing Editor, C&amp;EN Media Group)
</blockquote>

C&EN: Direct Analysis of Glycosylated Therapeutics

Direct Analysis of Glycosylated Therapeutics

New approach to glycoform fingerprinting that uses proton-transfer charge-reduction with gas-phase fractionation to analyze intact glycoproteins.

Are you ready to propel drug development and revolutionize the pharma industry?
On the quest to develop more effective drugs, the synergy between technology providers and scientists is paramount. Together, they generate reliable and reproducible results, accelerating new chemical entities through the pipeline. From research to commercialization, a continuous cycle of tests and workflows shapes the future, determining your success.
Discover new possibilities:
Unlock the potential of cutting-edge technology and master the art of making the right decisions. The 2-day event brings you interactive expert talks, enriching your knowledge and empowering you to embrace innovative techniques that save precious time at work. From the research of new markers to the drug development moving into non and GLP bioanalysis. Plan your next lab expansion with confidence.
Why attend?
<ul>
<li>Insightful expert talks: engage with 8 prominent speakers and key opinion leaders in the field
</li>
<li>Explore mass spectrometry in pharma: talks about research and quantitation of biomarkers, characterization of metabolites, drug quantitation and nitrosamine impurities, harness the power of mass spectrometry and plan your lab expansion with confidence
</li>
<li>Collaboration and networking: connect with like-minded professionals, share experiences, and build valuable connections within the industry
</li>
<li>Be the forefront of advancements: stay ahead of the competition by gaining insights into the latest trends and advancements in pharma technology
</li>
</ul>
<h3>Agenda Day 1: Wednesday, October 25</h3>
<h5>10:00 - 10:40 The Echo® MS system, a high throughout mass spectrometry, Revolution to accelerate hit finding and drug discovery</h5>
<ul>
<li>Celine Legros and Dany Jeanne Dit Fouque (Eurofins)</li>
</ul>
<h5>10:40 - 11:20 Qualification of lipid biomarker assays using chromatography with triple-quad mass spectrometry</h5>
<ul>
<li>Freddy Oosterbring (Ardena)</li>
</ul>
<h5>11:20 - 11:30 Break</h5>
<h5>11:30 - 12:10 Mass spectrometry, a useful aid in Alzheimer´s disease diagnosis</h5>
<ul>
<li>Jose Antonio Allué (Araclon)</li>
</ul>
<h5>12:10 - 12:50 LC-MS to analyze oligonucleotides: a tool for the characterization of new biotherapeutics</h5>
<ul>
<li>Margalida Artigues (IQS)</li>
</ul>
<h5>12:50 - 13:00 Final notes</h5>
<ul>
<li>Ferran Sanchez (SCIEX)</li>
</ul>
<blockquote>
Presenter: Celine Legros (Drug Discovery, Partnership Director, Eurofins Discovery)
</blockquote>
<blockquote>
Celine Legros, PhD, Drug Discovery Partnership Director, is deeply involved in the design of complex projects, including Hit-Finding, Hit-toLead and Lead-Op programs. Prior to joining Eurofins, Dr. Legros was Scientific Project Leader in the Screening Department at the Institut de Recherches Servier, France, where she was involved in neuroscience, cardio-metabolic diseases, immune-inflammation, and oncology projects, from HTS through to Lead-Optimization. Dr. Legros holds a Ph.D. in Animal Physiology (melatonin circanual rhythm and melatonin receptors) from the University of Tours, France, and completed a postdoctoral fellowship at the Blood Brain Barrier Group at King’s College London, UK.
</blockquote>
<blockquote>
Presenter: Dany Jeanne Dit Fouque (Development Analytic Engineer, Eurofins Cerep)
</blockquote>
<blockquote>
Dany Jeanne dit Fouque, PhD, is a Mass Spectrometry Analytical Development Engineer at Eurofins Cerep. He has 7 years of experience in analytical chemistry with in-depth knowledge in UHPLC-MS/MS method development, enzymatic reaction and MS-Binding using mass spectrometry. Prior to joining Eurofins, he worked in the academic sector on several R&amp;D projects to develop and optimize a new methodology using UHPLC-MSn experiments to identify and quantify isomeric/isobaric compounds in mixture. Dr. Jeanne dit Fouque received his Ph.D. in Mass Spectrometry from the University of Brest, France.
</blockquote>
<blockquote>
Presenter: Freddy Oosterbring (Senior Scientist, Deputy Director Laboratory, Ardena)
</blockquote>
<blockquote>
Freddy Oostebring, Manager Laboratory section chromatography and mass spectrometry at Ardena Bioanalysis. He holds a bachelor degree in Analytical Chemistry and has been working with triple quad mass spectrometry for more than 20 years. His expertise is in the field of method development for the analysis of small molecules, targeted lipids and peptides in biological matrices. Since 2019, he has been a member of the SCIEX Innovation Advisory Board.
</blockquote>
<blockquote>
Presenter: Jose Antonio Allué (Senior Scientist Mass Spectrometry Laboratory, R&amp;D Department, Araclon Biotech S.L., Ph.D. (Pharmacy) University of Barcelona, Spain.)
</blockquote>
<blockquote>
Twenty-five years in the field of Biological Mass Spectrometry, fifteen of them dedicated to research in Alzheimer´s Disease by HPLC-MS/MS (MALDI, IMS-MS, Orbitrap-MS, reTOF-MS, TOF/TOF-MS, Ion-Trap-MS and Triple Quadrupole-MS). Applications of both, targeted and untargeted, proteomic techniques in the fields of immunology, metabolism, pharmacokinetics and pharmacodynamics. Applications of High-Mass MALDI Mass Spectrometry for the analysis of protein complexes and vaccines. Label-free shotgun proteomics by Travelling Wave Ion Mobility Spectrometry coupled to TOF-MS. Applications of MS to the study of amyloid species in tissues and biofluids, including human, dog and transgenic mice models. Research focus: blood and cerebrospinal fluid amyloid biomarkers in Alzheimer´s Disease. Direct analysis of amyloid peptides in blood without immunoprecipitation enrichment.
</blockquote>
<blockquote>
Presenter: Margalida Artigues (Responsable de IQS SCIEX Demo Lab, Instituto Químico de Sarrià IQS)
</blockquote>
<blockquote>
Margalida Artigues earned her Ph.D. in Chemistry in 2019 from Ramon Llull University. She holds a Master&#39;s degree in Analytical Chemistry, as well as a Bachelor&#39;s degree in Chemistry, both from the same university. Since 2021, she has been leading the Mass Spectrometry Laboratory IQS-SCIEX Demo Lab, based in Barcelona, where she is an integral part of the research team at IQS Tech Transfer. In her current role, her mission is to promote research, facilitate technology transfer, and provide support in educational activities related to the LC-MS analytical technique.
</blockquote>
<blockquote>
Presenter: Emiliano de Dominicis (Chemistry Research Director, Mérieux NutriSciences)
</blockquote>
<blockquote>
Emiliano De Dominicis is a researcher with over twenty years of experience in food and pharmaceutical safety, following both private and academic sectors, and he is now Director of Chemical Research - Project Manager at Mérieux NutriSciences. With a Research and Development in Analytical Chemistry dedicated team, Emiliano is responsible for Mérieux NutriSciences Global Research Projects and Scientific Center. Moreover, Emiliano De Dominicis actively participates in funded scientific projects (regional, national and European), scientific congresses as speaker, and writes articles published in specialized scientific journals.
</blockquote>
<blockquote>
Presenter: Lukas Mogler (Sr Group Leader, Extractables and Leachables, Lonza DPS)
</blockquote>
<blockquote>
Dr. Lukas Mogler, Sr Group Leader Extractables and Leachables at Lonza DPS Basel Switzerland. He is a graduated diploma pharmacist holding a PhD from University of Freiburg, Germany. Worked in the field of Forensic Toxicology with focus on mass spectrometry and metabolism studies. Joined Lonza DPS in 2020, responsible for extractables and leachables and elemental impurities assessments.
</blockquote>
<blockquote>
Presenter: Ashwani Gaur (Senior Principal Scientist, Drug Metabolism and Pharmacokinetics, Syngene international Limited)
</blockquote>
<blockquote>
Ashwani Gaur, is Senior Principal scientist in Drug metabolism and Pharmacokinetics department of Syngene international Limited. Ashwani Joined Bioanalytical team in Ranbaxy research Lab soon after completing MS degree in Pharmaceutical Analysis from National Institute of Pharmaceutical Education and Research, India in 2004. Prior to Syngene, he worked in Advinus Therapeutics and Eurofins. Ashwani has contributed to small molecules drug-discovery projects internally and with large and medium size pharmaceutical companies around the globe specifically in lead identification/optimization stages. He leads a team of experts in LC-MS-based bioanalysis of small molecules, metabolites, prodrugs, biomarkers, complex bioanalysis involving chemical derivitisation and exposure determination new modalities like Protacs, ADC`s, oligonucleotides etc. in multiple biological matrices.
</blockquote>

Pharma conclave 2023 (Day 1)

Interactive expert talks, enriching your knowledge and empowering you to embrace innovative techniques that save precious time at work.

Are you ready to propel drug development and revolutionize the pharma industry?
On the quest to develop more effective drugs, the synergy between technology providers and scientists is paramount. Together, they generate reliable and reproducible results, accelerating new chemical entities through the pipeline. From research to commercialization, a continuous cycle of tests and workflows shapes the future, determining your success.
Discover new possibilities:
Unlock the potential of cutting-edge technology and master the art of making the right decisions. The 2-day event brings you interactive expert talks, enriching your knowledge and empowering you to embrace innovative techniques that save precious time at work. From the research of new markers to the drug development moving into non and GLP bioanalysis. Plan your next lab expansion with confidence.
Why attend?
<ul>
<li>Insightful expert talks: engage with 8 prominent speakers and key opinion leaders in the field
</li>
<li>Explore mass spectrometry in pharma: talks about research and quantitation of biomarkers, characterization of metabolites, drug quantitation and nitrosamine impurities, harness the power of mass spectrometry and plan your lab expansion with confidence
</li>
<li>Collaboration and networking: connect with like-minded professionals, share experiences, and build valuable connections within the industry
</li>
<li>Be the forefront of advancements: stay ahead of the competition by gaining insights into the latest trends and advancements in pharma technology
</li>
</ul>
<h3>Agenda Day 2: Thursday, October 26</h3>
<h5>10:00 - 10:40 Case studies from bioanalytical lab in DMPK, Syngene: SCIEX 7500 system and beyond</h5>
<ul>
<li>Ashwani Gaur (Syngene International Ltd)</li>
</ul>
<h5>10:40 - 11:20 Challenges in quantification of NDSRI’s</h5>
<ul>
<li>Dama Venugopal Rao (Dr. Reddy&#39;s Laboratories)</li>
</ul>
<h5>11:20 - 11:30 Break</h5>
<h5>11:30 - 12:10 Nitrosamine impurities in dermal products: from APIs and their salts (secondary amines) evaluations through analytical chemistry and mass spectrometry</h5>
<ul>
<li>Emiliano de Dominicis (Merieux)</li>
</ul>
<h5>12:10 - 12:50 Extractables and leachables assessments in biologics manufacturing</h5>
<ul>
<li>Lukas Mogler (Lonza)</li>
</ul>
<h5>12:50 - 13:00 Final notes</h5>
<ul>
<li>Ferran Sanchez (SCIEX)</li>
</ul>
<blockquote>
Presenter: Celine Legros (Drug Discovery, Partnership Director, Eurofins Discovery)
</blockquote>
<blockquote>
Celine Legros, PhD, Drug Discovery Partnership Director, is deeply involved in the design of complex projects, including Hit-Finding, Hit-toLead and Lead-Op programs. Prior to joining Eurofins, Dr. Legros was Scientific Project Leader in the Screening Department at the Institut de Recherches Servier, France, where she was involved in neuroscience, cardio-metabolic diseases, immune-inflammation, and oncology projects, from HTS through to Lead-Optimization. Dr. Legros holds a Ph.D. in Animal Physiology (melatonin circanual rhythm and melatonin receptors) from the University of Tours, France, and completed a postdoctoral fellowship at the Blood Brain Barrier Group at King’s College London, UK.
</blockquote>
<blockquote>
Presenter: Dany Jeanne Dit Fouque (Development Analytic Engineer, Eurofins Cerep)
</blockquote>
<blockquote>
Dany Jeanne dit Fouque, PhD, is a Mass Spectrometry Analytical Development Engineer at Eurofins Cerep. He has 7 years of experience in analytical chemistry with in-depth knowledge in UHPLC-MS/MS method development, enzymatic reaction and MS-Binding using mass spectrometry. Prior to joining Eurofins, he worked in the academic sector on several R&amp;D projects to develop and optimize a new methodology using UHPLC-MSn experiments to identify and quantify isomeric/isobaric compounds in mixture. Dr. Jeanne dit Fouque received his Ph.D. in Mass Spectrometry from the University of Brest, France.
</blockquote>
<blockquote>
Presenter: Freddy Oosterbring (Senior Scientist, Deputy Director Laboratory, Ardena)
</blockquote>
<blockquote>
Freddy Oostebring, Manager Laboratory section chromatography and mass spectrometry at Ardena Bioanalysis. He holds a bachelor degree in Analytical Chemistry and has been working with triple quad mass spectrometry for more than 20 years. His expertise is in the field of method development for the analysis of small molecules, targeted lipids and peptides in biological matrices. Since 2019, he has been a member of the SCIEX Innovation Advisory Board.
</blockquote>
<blockquote>
Presenter: Jose Antonio Allué (Senior Scientist Mass Spectrometry Laboratory, R&amp;D Department, Araclon Biotech S.L., Ph.D. (Pharmacy) University of Barcelona, Spain.)
</blockquote>
<blockquote>
Twenty-five years in the field of Biological Mass Spectrometry, fifteen of them dedicated to research in Alzheimer´s Disease by HPLC-MS/MS (MALDI, IMS-MS, Orbitrap-MS, reTOF-MS, TOF/TOF-MS, Ion-Trap-MS and Triple Quadrupole-MS). Applications of both, targeted and untargeted, proteomic techniques in the fields of immunology, metabolism, pharmacokinetics and pharmacodynamics. Applications of High-Mass MALDI Mass Spectrometry for the analysis of protein complexes and vaccines. Label-free shotgun proteomics by Travelling Wave Ion Mobility Spectrometry coupled to TOF-MS. Applications of MS to the study of amyloid species in tissues and biofluids, including human, dog and transgenic mice models. Research focus: blood and cerebrospinal fluid amyloid biomarkers in Alzheimer´s Disease. Direct analysis of amyloid peptides in blood without immunoprecipitation enrichment.
</blockquote>
<blockquote>
Presenter: Margalida Artigues (Responsable de IQS SCIEX Demo Lab, Instituto Químico de Sarrià IQS)
</blockquote>
<blockquote>
Margalida Artigues earned her Ph.D. in Chemistry in 2019 from Ramon Llull University. She holds a Master&#39;s degree in Analytical Chemistry, as well as a Bachelor&#39;s degree in Chemistry, both from the same university. Since 2021, she has been leading the Mass Spectrometry Laboratory IQS-SCIEX Demo Lab, based in Barcelona, where she is an integral part of the research team at IQS Tech Transfer. In her current role, her mission is to promote research, facilitate technology transfer, and provide support in educational activities related to the LC-MS analytical technique.
</blockquote>
<blockquote>
Presenter: Emiliano de Dominicis (Chemistry Research Director, Mérieux NutriSciences)
</blockquote>
<blockquote>
Emiliano De Dominicis is a researcher with over twenty years of experience in food and pharmaceutical safety, following both private and academic sectors, and he is now Director of Chemical Research - Project Manager at Mérieux NutriSciences. With a Research and Development in Analytical Chemistry dedicated team, Emiliano is responsible for Mérieux NutriSciences Global Research Projects and Scientific Center. Moreover, Emiliano De Dominicis actively participates in funded scientific projects (regional, national and European), scientific congresses as speaker, and writes articles published in specialized scientific journals.
</blockquote>
<blockquote>
Presenter: Lukas Mogler (Sr Group Leader, Extractables and Leachables, Lonza DPS)
</blockquote>
<blockquote>
Dr. Lukas Mogler, Sr Group Leader Extractables and Leachables at Lonza DPS Basel Switzerland. He is a graduated diploma pharmacist holding a PhD from University of Freiburg, Germany. Worked in the field of Forensic Toxicology with focus on mass spectrometry and metabolism studies. Joined Lonza DPS in 2020, responsible for extractables and leachables and elemental impurities assessments.
</blockquote>
<blockquote>
Presenter: Ashwani Gaur (Senior Principal Scientist, Drug Metabolism and Pharmacokinetics, Syngene international Limited)
</blockquote>
<blockquote>
Ashwani Gaur, is Senior Principal scientist in Drug metabolism and Pharmacokinetics department of Syngene international Limited. Ashwani Joined Bioanalytical team in Ranbaxy research Lab soon after completing MS degree in Pharmaceutical Analysis from National Institute of Pharmaceutical Education and Research, India in 2004. Prior to Syngene, he worked in Advinus Therapeutics and Eurofins. Ashwani has contributed to small molecules drug-discovery projects internally and with large and medium size pharmaceutical companies around the globe specifically in lead identification/optimization stages. He leads a team of experts in LC-MS-based bioanalysis of small molecules, metabolites, prodrugs, biomarkers, complex bioanalysis involving chemical derivitisation and exposure determination new modalities like Protacs, ADC`s, oligonucleotides etc. in multiple biological matrices.
</blockquote>

Pharma conclave 2023 (Day 2)

Mass Spectrometry Imaging (MSI) is a technique that allows chemical information to be obtained directly or via the use of matrices from a wide range of surfaces.
MS Imaging provides information on the spatial distribution of molecules at or near the surface. Imaging provides beautiful and information-rich images that allow scientists to answer the fundamental question: “Where is this component in my sample?”
In this webinar series, we will examine the basics of MS imaging, compare the techniques of untargeted and targeted MS Imaging and the information that can be gained from each, and end with an interview from Dr. Ryan Leib (Stanford University) and Dr. Roy Martin (Waters Corporation) on the practicalities of setting up a MS Imaging Core lab.
Who Should Attend: 
<ul>
<li>Any scientist, lab managers or lab directors looking to expand (or refresh) their knowledge of MS Imaging.</li>
</ul>
<h4>Part Three – October 31st, 2023: Building an MS Imaging Facility</h4>
In the final session of the series, we will have a roundtable with Dr. Ryan Leib (Stanford University) and Dr. Roy Martin (Waters Corporation) where we will discuss the steps necessary to set up an MS imaging core lab and answer questions such as: “who runs this type of lab?” and “who are the main customers?”.
<blockquote>
Presenter: Roy Martin (Principal Field Marketing Manager, Waters Corporation)
</blockquote>
<blockquote>
Dr. LeRoy B. Martin, III is the Principal Field Marketing Manager for Biological Mass Spectrometry at Waters Corporation. His primary role is developing and promoting advanced mass spectrometry solutions in the Americas. He is also charged with evaluating and integrating new technologies and methods in collaborations and product development. Most recently, his focus has been on molecular imaging mass spectrometry and implementation of advances in ion mobility technology. Other research interests include complex mixture quantitative proteomics and structural biology using mass spectrometry. Roy received a BS in Chemistry from Davidson College and a Ph.D. in Analytical Chemistry from North Carolina State University.
</blockquote>
<blockquote>
Presenter: Ryan Leib (Director of Research, Stanford University Mass Spectrometry Laboratory)
</blockquote>
<blockquote>
Ryan Leib is Director of Research for the Stanford University Mass Spectrometry Laboratory. Ryan received his B.S. in Biochemistry from the University of Tulsa (Tulsa, OK), with a focus on LC/MS methods development for natural products discovery. In 2010, he received his Ph.D. in Chemistry from the University of California at Berkeley investigating ionic cluster formation and energetics in Professor Evan Williams’ mass spectrometry laboratory. Prior to joining SUMS in 2014, Ryan developed mass spectrometric analyses for complex mixtures as a Project Leader at SRI International, a non-profit contract R&amp;D firm based in Silicon Valley.
</blockquote>
<blockquote>
Presenter: Kieron Faherty, Ph.D. (Separations and Mass Spectrometry Field Marketing Manager, Waters Corporation)
</blockquote>
<blockquote>
Kieron Faherty is the Separations and Mass Spectrometry Field Marketing Manager for the Americas at Waters Corporation. He received his B.Sc. (Hons) in Chemistry from the University of Reading (Reading, Berkshire, UK) and his doctorate in Chemistry from the University of Massachusetts (Amherst, MA). He has held several field-based positions at Waters, most recently as a Field Applications Specialist focused on biopharmaceutical applications using Time-of-Flight mass spectrometry instrumentation.
</blockquote>

Waters Corporation: Building an MS Imaging Facility

Building an MS Imaging Facility

The steps necessary to set up an MS imaging core lab and answer questions such as: “who runs this type of lab?” and “who are the main customers?”.

During drug metabolite identification (Met ID) studies collision-induced dissociation (CID) is the most commonly used fragmentation technique for LC-MS experiments.
Many conjugation metabolites are found to have multiple bonding potentials to parent drugs. It is a great challenge to locate the bonding sites by CID due to the information lost by highly selective cleavage on these bonds. 
The novel electron-activated dissociation (EAD) is a recently developed technology on the SCIEX ZenoTOF 7600 system. From a single LC-MS/MS experiment CID and EAD data can be collected, providing information rich fragmentation spectra. The additional information can help in confident localization and identification of metabolites compared to CID alone. These fragments can be crucial to locate the metabolic modification sites, such as conjugations. 
In this study, the application of EAD in drug metabolite profiling is explored. The efficiency in the structural elucidation of conjugation metabolites is compared with that of CID.
Webinar Learning Objectives:
<ul>
<li>Learn how EAD can be advantageous in confident identification and localization of drug metabolites
</li>
<li>Discover the sensitivity of the Zeno trap technology in the identification of the low abundant metabolites
</li>
<li>Explore the capabilities of the Molecule Profiler software in processing EAD and CID data for drug metabolite identification
</li>
</ul>
<blockquote>
Presenter: Ming Yao (Principal Scientist, CPPDB, Bristol-Myers Squibb)
</blockquote>
<blockquote>
Ming Yao currently works at Bristol-Myers Squibb (BMS). He received his B.Sc. from Henan University, and his M.Sc. from the Chinese Academy of Preventive Medicine China. After graduation, he worked at the Institute of Occupational Medicine as an associate professor.
</blockquote>
<blockquote>
As a visiting Associate Professor, he conducted research for bioactivation of chemicals at Merck as well as the University of Western Ontario. After then, he joined BMS and he was responsible for designing and conducting in vitro and in vivo biotransformation studies for multiple programs to support both development and discovery projects. Most recently, he has also been involved in the development of protein drugs, such as the antibody drug conjugates (ADCs) and biotransformation of biologics.
</blockquote>
<blockquote>
Ming has over 28 years of experiences in the pharmaceutical industry and has over 50 publications and 5 book chapters covering new technologies of mass spectrometry and its applications in drug metabolism.
</blockquote>
<blockquote>
Presenter: Rahul Baghla (Manager Pharma Applications, SCIEX)
</blockquote>
<blockquote>
Rahul Baghla, Manager Pharma Applications is a research scientist with 12+ years of experience in various applications of mass spectrometry delivering in Pharma/Biopharma/CRO industries. He is specialised in implementing new mass spectrometry technologies in bioanalytical/analytical method development/validation, drug discovery, ADME assays and clinical studies.
</blockquote>
<blockquote>
He has supported various functions within pharma industry including nutrition, wellness, and oral care based clinical trial studies over the years. Rahul has master’s degree in pharmaceutical analysis, master’s in business administration and a professional diploma in clinical research.
</blockquote>
<blockquote>
He is responsible for continuous engagement with pharmaceutical community to identify major analytical challenges, provide solutions and to find significant analytical opportunities for SCIEX.
</blockquote>

SCIEX: Discover how Bristol-Myers Squibb uses electron-activated dissociation (EAD) to confidently identify drug metabolites and localize site of metabolism.

Discover how Bristol-Myers Squibb uses electron-activated dissociation (EAD) to confidently identify drug metabolites and localize site of metabolism.

Learn how EAD can be advantageous in confident identification and localization of drug metabolites.

LC/MS EAD & drug metabolites & localization of metabolism

Over the last few years, spatial biology has refined the understanding of coordinated biological processes that govern how systems both thrive and become vulnerable to disease.
The latest tools offer advanced images that track the location and types of proteins and RNA across tissue microdomains and cellular phenotypes using a variety of detection techniques but lack the ability to see other post-transcriptional processes defined by metabolites and glycans. MALDI Imaging is a true multiomics technique that allows for spatial determination of metabolites and lipids in tissue, as well as expanding targeted analysis to small molecules, glycans, and proteins. The addition of MALDI-2 and microGRID technology enables imaging for maximum biological information at previously unreachable sensitivity and robust (sub)cellular resolution.
This webinar will introduce how Bruker’s new MALDI HiPLEX-IHC Imaging workflow delivers greater speed and field-of-view for multiplexed protein imaging in tissue, while providing thousands of untargeted molecular images that enable deeper tissue subtyping. The combination of protein spatial localization combined with metabolites and glycans offers a new pathway for coordinated biomarker discovery to complement existing spatial techniques.
What to expect?
<ul>
<li>Live presentation from Bruker’s experts to see ease of use of the timsTOF fleX platform, new MALDI HiPLEX-IHC workflows and highlighting user stories, including focus on improved spatial resolution with microGRID, improved sensitivity with MALDI-2, improved separation selectivity with trapped ion mobility and comprehensive software solutions</li>
</ul>
Who should attend?
<ul>
<li>Anyone using or interested in using tools for spatial biology discovery or translation
</li>
<li>Scientists &amp; researchers interested in expanding their workflows to the spatial dimension, scientists working with spatial distribution of small molecule biologics
</li>
<li>MALDI Imaging users wanting to expand their workflows
</li>
<li>Anyone interested in learning more about MALDI Imaging capabilities
</li>
</ul>
<blockquote>
Presenter: Kate Stumpo, Ph.D. (Senior Market Manager Imaging, Bruker, Billerica, MA, USA)
<ul>
<li>Introduction and welcome to MALDI Imaging </li>
<li>Spatial biology meets Mass Spectrometry in cancer research </li>
<li>MALDI Imaging utility in neurological research</li>
</ul>
</blockquote>
<blockquote>
Presenter: Corinna Henkel, Ph.D. (Application Scientist Imaging, Bruker, Bremen, Germany)
<ul>
<li>MALDI HiPLEX-IHC workflow technical introduction</li>
<li>Software solutions for multiomics integration</li>
</ul>
</blockquote>
<blockquote>
Presenter: Bjoern Wendik, Ph.D. (Business Development Manager, Bruker, Bremen, Germany)
<ul>
<li>Bridging non-MS imaging to the MALDI world</li>
<li>Automation, workflow and relevance for future clinical applications</li>
</ul>
</blockquote>

Bruker: Redefining Hiplexed Spatial Multiomics

Redefining Hiplexed Spatial Multiomics

How Bruker’s new MALDI HiPLEX-IHC Imaging workflow delivers greater speed and field-of-view for multiplexed protein imaging in tissue.

In this webinar, we will present end-to-end solutions for biopharma lab workflows with a focus on multiple mass spectrometry- based analysis techniques, ranging from SQ, TQ, TOF and Q-TOF.
A broad portfolio in sample prep automation for protein therapeutics allows for highly reproducible results in the starting point of the analysis. A broad range of consumables and columns will be presented, leading into the subsequent separation via HPLC and detection by mass spectrometry.
The 6545XT AdvanceBio was particularly developed for intact protein analysis, and the ultra-high vacuum and large molecule autotune led to excellent sensitivity in denatured and native applications, allowing quantitation on the intact protein level as well as ADR calculations. Peptide mapping and glycan analysis results, along with the confirmation of oligonucleotide sequences using Q-TOF-based workflows, will be presented.
We will also highlight the ultrahigh performance of the novel 6495 triple quadrupole LC/MS system (G6495D) with MassHunter Workstation 12.1 for comprehensive multiplexed protein quantification. Artificial intelligence (AI)-based SWARM autotune and enhanced system features provide seamless protein quantification method optimization, ultimate analytical sensitivity, and high analytical precision as well as user-friendly instrument care and maintenance.
Lastly, we will show results from oligonucleotides and proteins analyzed on LC/MS single quadrupole and Time of Flight (TOF) instruments, the latest scientific applications, and recent method improvements.
<blockquote>
Presenter: Ian Edwards, Ph.D. (LC/TQ Portfolio Product Manager, Agilent Technologies Inc.)
</blockquote>
<blockquote>
Ian holds a PhD from the Centre for Proteome Research at the University of Liverpool. He has spent time as a pre- and post-sales MS applications specialist focused on MS imaging and proteomics, as a field marketing manager for -omics, and as a global pharmaceutical marketing manager. Ian joined Agilent recently as LC/TQ Product Manager.
</blockquote>
<blockquote>
Presenter: Russell Burge, Ph.D. (LC/SQ and LC/TOF Portfolio Product Manager, Agilent Technologies Inc.)
</blockquote>
<blockquote>
Russell earned a PhD in biochemistry and molecular biology from Scripps Research. He has extensive experience in the R&amp;D of biomolecules and biopharmaceuticals, and the implementation of automated workflows. Russell has acted as a Product Manager for various products in Life Science and Industrial Markets, and he currently manages the LC/MS SQ and LC/MS TOF product portfolios at Agilent.
</blockquote>
<blockquote>
Presenter: Christian Klein, Ph.D. (LC/Q-TOF Portfolio Product Manager, Agilent Technologies Inc.)
</blockquote>
<blockquote>
With an education in Chemistry, Chris Klein received his Ph.D. in 2005 at the Max-Planck-Institute for Biochemistry in Martinsried, Germany. He joined Agilent Technologies in 2010 as the lead chemist in the LC/Q-TOF R&amp;D team. In 2018 Chris jointed the marketing team as Portfolio Product Manager, responsible for LC/Q-TOF and Ion Mobility.
</blockquote>
<blockquote>
Presenter: Róisín Murtagh (Editor, Wiley)
</blockquote>
<blockquote>
Róisín Murtagh has been an editor for Wiley Analytical Science since 2021. She holds a science degree from Maynooth University, Ireland, and an MSc in Medicinal Chemistry from the Open University, UK. With a background encompassing over 10 years of experience in analytical science, she has actively contributed to both industry and academic research.
</blockquote>

Wiley: Intelligent LC/MS tools for quantitation and characterization of biopharmaceuticals

Intelligent LC/MS tools for quantitation and characterization of biopharmaceuticals

End-to-end solutions for biopharma lab workflows with a focus on multiple mass spectrometry- based analysis techniques, ranging from SQ, TQ, TOF and Q-TOF.**

LC/MS quantitation & characterization of biopharmaceuticals

Single-cell proteomics by mass spectrometry can provide valuable insights into distinct cell states and signaling patterns present in a cell population. However, carrying out proteomics profiling from the limited amount of material encapsulated in an individual cell presents significant challenges.
Tremendous efforts have been made to optimize all aspects of single-cell proteomics by mass spectrometry, with the aim of minimizing losses during sample preparation and maximizing sensitivity of data acquisition. Nevertheless, continuous development is needed to increase both the quantifiable proteome depth per cell, the quantitative accuracy and precision of those measurements, and the number of cells measured per unit time.
This webcast will present recently-developed approaches, ranging from sample preparation and chromatographic separation to advanced data acquisition, data interpretation and visualization methods. Advances in instrumentation, including the novel <a href="https://lcms.cz/products/836">Orbitrap Astral MS</a>, and how to use both TMTPro-labeled and label-free approaches, will be presented, showcasing the application of these methods to biomedical questions, and providing an overview of the current technological state of the field.
<h5>Learn how to:</h5>
<ul>
<li>Prepare single cells for analysis by mass spectrometry</li>
<li>Improve the sensitivity and throughput of single-cell proteomics analysis</li>
<li>Implement both label-free and labeled quantitative approaches to single-cell proteomics</li>
</ul>
<blockquote>
Presenter: Dr. Erwin Schoof (Associate Professor, Department of Biotechnology and Biomedicine, Section for Protein Science and Biotherapeutics, Cell Diversity Lab, Technical University of Denmark)
</blockquote>

Metrolab SA: Single-cell proteomics on the Orbitrap Astral MS for the exploration of cell heterogeneity

Single-cell proteomics on the Orbitrap Astral MS for the exploration of cell heterogeneity

This webcast will present recently-developed approaches in single-cell proteomics including the novel Orbitrap Astral MS.

LCMS webinars focusing on LC/HRMS - page 30