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

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

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

Webinars LabRulezLCMS Week 07/2026

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

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

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<h5><strong>Key Learning Points:</strong></h5><ul><li>Understand best practices upon opening a new LC Column</li><li>Learn how to clean and regenerate an LC Column</li><li>Find out about additional products and practices that can be used to minimize contamination getting onto LC columns</li></ul><h5><strong>Who Should Attend:</strong></h5><ul><li>Any LC user who would like to ensure that their LC columns are properly cared for to make sure to get most life out of it that is possible.</li></ul><blockquote><p><strong>Presenter:</strong> Genevieve Hodson (Senior Manager, Technical Support &amp; Applications, Phenomenex)</p><p>Genevieve graduated from the University of Texas with a BS in Chemistry located in her home town of Austin Texas. She spent 2 years of her undergraduate performing research in an Organic Chemistry Lab synthesizing intermediates. Out of school she spent 4 years as an Analytical Chemist in the QC and R&amp;D Department of Cerilliant (a Sigma Millipore Company). There she worked with many analytical instruments but became an expert at LC by performing purity analysis, customer specific methods, validations, qc testing and stability studies on a wide range of small molecules including pharmaceuticals, pesticides, explosives and illegal substances. From there she moved to Los Angeles California where she worked at Johnson and Johnson and then a small dietary supplement company. After Genevieve spent a year living abroad in Israel raising her first son, she moved back to LA where she got hired as a Technical Specialist at Phenomenex. At Phenomenex she enjoys continuing to learn about chromatography every day through helping customer with all their chromatography needs!</p></blockquote>

Phenomenex: How to Take Care of Your LC Column

How to Take Care of Your LC Column

Learn about the best practices upon opening your new LC Column, how to clean and regenerate, and additional products and practices...

<p><strong>Measuring scattering samples with UV-VIS-NIR can be challenging for basic instruments. These samples will have diffuse reflectance or transmission and less light hitting your detector.</strong></p><p>In this presentation, we will discuss diffuse reflectance accessories (DRAs) for collecting all light in a measurement as well as Agilent's universal measurement accessory (UMA) for measuring the angular distribution of the reflected light.</p><blockquote><p><strong>Presenter:</strong> Scott Melis, PhD (Application Scientist, Agilent Technologies, Inc.)</p><p>Scott Melis has a PHD in Physics from Georgetown University in Washington, DC and started with Agilent in 2021 as a Molecular Spectroscopy Application Scientist. In his graduate work, Scott studied nanoparticle formation and growth for a variety of applications. Projects that he worked with include developing processes to deposit and characterize semiconducting molecular nano-cocrystals for use in optoelectronic devices as well as controlling polymer nanoparticle size through rapid mixing conditions.</p></blockquote>

Agilent Technologies: Measuring Diffuse Powders and Films With UV-VIS-NIR

Measuring Diffuse Powders and Films With UV-VIS-NIR

We will discuss diffuse reflectance accessories (DRAs) as well as Agilent's universal measurement accessory (UMA).

<div><h4><strong>2026 AQbD Symposium Day 1 - Pharma Small Molecules</strong></h4><p>Staying ahead of regulatory change is a challenge. Evolving guidelines like ICH Q14, Q2(R2), USP &lt;1220&gt;, and the upcoming ICH M4Q(R2) and USP &lt;1225&gt; are reshaping expectations for analytical methods. Risk management and fit-for-purpose principles are now critical for compliance. Join us to explore how Analytical Quality by Design (AQbD) can help you design robust methods, streamline transfers, and meet today’s stringent small molecule and biopharmaceutical requirements.&nbsp;</p><h5><strong>Why Attend:</strong></h5><ul><li>Learn how to apply AQbD principles to the development of robust, risk-based analytical procedures.</li><li>Use DoE tools to identify risks during method transfer and migration.</li><li>Gain practical insights from industry experts on case studies to improve analytical testing reliability.</li></ul><h4><strong>Session 1:</strong></h4><h5><strong>Pharma Small Molecules Presentations Practical elements from ICHQ14, Q2R2 and USP Enhanced Approach » and Practical Tools to Reduce Analytical Risks&nbsp;</strong></h5><ul><li>Gérald de Fontenay, Scientific Director, CEBIPHAR</li></ul><h5><strong>AQbD and DOE Across Pharma Analytical Development</strong></h5><ul><li>Davide Messini, Analytical Development Senior/Scientist, F.I.S. - Fabbrica Italiana Sintetici S.p.A.</li></ul><h5><strong>AQbD Approaches for GLP-1 RA Impurity Profiling</strong></h5><ul><li>Pawel Bigos, Senior Scientist, Waters Corporation</li></ul><blockquote><p><strong>Presenter:</strong> Gérald de Fontenay (Directeur Scientifique et Technique, CEBIPHAR)</p><p>For more than 25 years, Gérald has held key positions within service companies (analytical CROs and CDMOs). He is currently Scientific and Technical Director at CEBIPHAR, where he ensures the highest possible reliability of the results generated both in CEBIPHAR’s laboratories and in those of its clients.</p><p>He provides his expertise in the validation, verification, and transfer of analytical methods to support CEBIPHAR’s project managers and clients, helping to accelerate the implementation of new projects at production sites and to ensure the compliance of reports.</p><p><strong>Presenter:</strong> Davide Messini (Analytical Development Senior/Scientist, F.I.S. - Fabbrica Italiana Sintetici S.p.A.)</p><p>Degree in Chemistry (Padova). He has more than 20 years of experience in analytical chemistry in active pharmaceutical ingredients (API) manufacturing environment. He started in cGMP quality control as a QC analyst and then as R&amp;D analyst in analytical development department. Since 2010 he is responsible for the analytical development related to the manufacturing of API (small molecules) from lab to commercial scale developing and testing all analytical methods suitable for the quality assessment of the substance. Expertise in all common instrumentation used in pharma environment, he ensures the quality of the analytical methods, analytical development strategy, robustness tests and all related cGMP aspects.</p><p><strong>Presenter:</strong> Pawel Bigos (Senior Scientist, Waters Corporation)</p><p>Pawel Bigos is a Senior Scientist at Waters Corporation in the QA/QC Biologics group in Milford, Massachusetts. He holds a Bachelor of Science degree in Chemistry from the University of South Florida. Prior to Waters, Pawel gained valuable experience at Frequency Therapeutics, Novartis, and Symbiotic Research. Since joining Waters in 2022, he has concentrated on biomolecule separations and plays a critical role in providing analytical support in the development, commercialization, and application of Waters innovative products.</p></blockquote></div>

Waters Corporation: 2026 AQbD Symposium - Day 1 - Pharma Small Molecules

2026 AQbD Symposium - Day 1 - Pharma Small Molecules

Learn how AQbD and new ICH/USP guidelines enhance small-molecule method development, risk control, and lifecycle management at the 2026 AQbD Symposium.

2026 AQbD Symposium - Pharma Small Molecules

<h4><strong>How about a 30 minute coffee break along with a taste of Empower?</strong></h4><h4><strong>Here you go!</strong></h4><h5><strong>Short session, big results</strong></h5><p>Learn quick, impactful tricks to make your Empower Software reports smarter and more insightful. Whether you’re aiming for compliance or clarity, these practical hacks will help you save time and elevate your reporting. A short session – for big results.</p><h5><strong>What will you learn?</strong></h5><ul><li>Save time instantly – Discover techniques that dramatically reduce reporting effort</li><li>Boost report quality – Create clear reports that are more professional and easier to understand</li><li>Stay compliant with ease – Integrate regulatory requirements without stress</li></ul><p><i>Reserve your spot today and make your Empower Software reports shine!</i></p><blockquote><p><strong>Presenter: </strong>Ralf Schröder (Informatics Market Development Manager)</p><p><strong>Presenter:&nbsp;</strong>Carsten Fischer (Informatics Product Marketing, EMEA)</p><p><strong>Presenter:&nbsp;</strong>Ilse Hoes (Solutions Manager, Informatics at Waters Europe)</p></blockquote>

Waters Corporation: Informatics series #30 Empower Reports - Simple & Smart

Informatics series #30 Empower Reports - Simple & Smart

Learn quick, impactful tricks to make your Empower Software reports smarter and more insightful. 

Informatics series #30 Empower Reports 

<p><strong>Accurate mass fundamentals breaks down the barriers of complexity, demystifies misconceptions, and provides helpful tips on how to improve your data quality.</strong></p><p>Whether you already use accurate mass spectrometry and are looking to grow your knowledge or are currently working with nominal mass spectrometry and are thinking about making the switch, this webinar series will show you how accurate mass can simplify your workflow, clarify your data, and give you greater confidence in every result.</p><p>Sign up today to discover the practical advantages of accurate mass spectrometry.</p><h4><strong>Session 2: From theory to practical workflows</strong></h4><ul><li>See how accurate mass integrates into everyday workflows</li><li>Confidently interpret HRMS data</li><li>Build robust methods with automation to simplify complex analyses</li></ul>

Accurate mass fundamentals - From theory to practical workflows

How accurate mass spectrometry works in real workflows. Session 2 focuses on HRMS data interpretation, method robustness, and automation for complex analyses.

Accurate mass fundamentals - From theory to practice

<div><h4><strong>2026 AQbD Symposium Day 2 - Biopharmaceutical</strong></h4><p>Staying ahead of regulatory change is a challenge. Evolving guidelines like ICH Q14, Q2(R2), USP &lt;1220&gt;, and the upcoming ICH M4Q(R2) and USP &lt;1225&gt; are reshaping expectations for analytical methods. Risk management and fit-for-purpose principles are now critical for compliance. Join us to explore how Analytical Quality by Design (AQbD) can help you design robust methods, streamline transfers, and meet today’s stringent small molecule and biopharmaceutical requirements.&nbsp;</p><h5><strong>Why Attend:</strong></h5><ul><li>Learn how to apply AQbD principles to the development of robust, risk-based analytical procedures.</li><li>Use DoE tools to identify risks during method transfer and migration.</li><li>Gain practical insights from industry experts on case studies to improve analytical testing reliability.</li></ul><h4>Agenda</h4><h5><strong>Incorporating Analytical Quality by Design in Early Phase Development of mAbs and ADCs&nbsp;</strong></h5><ul><li>Mark Eggink, Principal Scientist, Analytical Development and Quality Control, Byondis</li></ul><h5><strong>Application of Analytical Quality by Design Principles to the Analysis of Nucleic Acids using an Innovative Dual Gradient Approach</strong></h5><ul><li>Ricardo Gonçalves, Senior Analytical Scientist, Hovione</li></ul><h5><strong>Leveraging AQbD Principles for Efficient Development of a Targeted Assay Method for Routine Monitoring of Mannose-5 Glycans Using Fluorescence Detection</strong></h5><ul><li>Pawel Bigos, Senior Scientist, Waters Corporation</li></ul><blockquote><p><strong>Presenter:</strong> Mark Eggink, Ph.D. (Principal Scientist, Analytical Development and Quality Control, Byondis)</p><p>Mark Eggink, PhD, is Principal Scientist at Byondis, where he is responsible for analytical support for process development, method development and validation, batch release and stability testing of monoclonal antibodies and antibody drug conjugates.</p><p><strong>Presenter: </strong>Ricardo Gonçalves (Senior Analytical Scientist, Hovione)</p><p><strong>Presenter: </strong>Udayabagya (Bud) Halim (Sr. Marketing Analyst, Waters Corporation)</p><p>Bud Halimis a senior marketing analyst at Waters | Wyatt Technology with a PhD in physical chemistry from UCLA. He began his career teaching biochemistry and chemistry and contributing to laboratory manuals before transitioning into the scientific instrumentation industry as an applications scientist. At Waters, he supports researchers in the characterization of peptides, biologics, lipid nanoparticles (LNPs), and viral vectors.</p></blockquote></div>

Waters Corporation: 2026 AQbD Symposium - Day 2 - Biopharmaceutical

2026 AQbD Symposium - Day 2 - Biopharmaceutical

Join Day 2 of the 2026 AQbD Symposium to learn how AQbD enables compliant, risk-based biopharmaceutical analytics under evolving ICH and USP guidelines.

2026 AQbD Symposium - Biopharmaceutical

<div><div container-id="cq-colctrl-lt0" comp-id="A1"><div><p><strong>Preparative LC is an indispensable technique for compound purification across many industries. This webinar delivers practical, ready-to-use tips—from smart column selection to smooth scale-up from analytical to preparative workflows—helping you improve yield, purity, and throughput right away.</strong></p><h4><strong>Who should view it?</strong></h4><p>Laboratory technicians, researchers, and scientists seeking to better understand how to facilitate the analytical-to-preparative chromatography workflow.</p><h4><strong>By attending this webinar, you will:</strong></h4><ul><li>Gain tips for selecting columns and systems in preparative chromatography</li><li>Discover best practices and considerations for scale-up</li><li>Learn methods to streamline preparative workflows</li></ul><blockquote><p><strong>Presenter: </strong>Daiki Fujimura (Assistant Manager, Labo Consumables, Shimadzu Corporation)</p><p>Daiki Fujimura majored in analytical chemistry at Meiji University in Tokyo, Japan, and joined Shimadzu Corporation in 2015. He has over 10 years of experience as an application chemist specializing in liquid chromatography.</p></blockquote></div></div></div>

SeparationScience: Fast Wins: Preparative LC Tips for Beginners Ready to Use Tomorrow

Fast Wins: Preparative LC Tips for Beginners Ready to Use Tomorrow

Discover how preparative LC can streamline your analytical workflows for compound purification.

Preparative LC Tips for Beginners Ready to Use Tomorrow

<div><h4><strong>Transform Lab Automation Connectivity</strong></h4><p>Join our exclusive webinar to discover how the <strong>Waters OneLab™ Secured Deployment Solution</strong> takes you from box to bench.</p><p>Your new <strong>Waters™ Andrew+ Robot</strong> has arrived, and you’re ready to automate right away with no IT support required. With intuitive technology and clear guidance, you’ll simplify setup and be on your path to impact in no time.</p><p>When you’re ready to connect OneLab™ Software with <strong>Empower™, MassLynx™, or waters_connect™</strong>, simply include our IT installation documentation with your request. Your IT partner will be ready to make the connection.</p><p>It’s simple, secure, Windows®-based, and designed to isolate the network connection from Andrew+ Robot, now you can automate with confidence.</p><h5><strong>Learn how OneLab Secured Deployment Solution architecture:</strong></h5><ul><li>Enables cybersecurity and delivers enterprise-ready performance</li><li>Accelerates IT implementation with ready-to-use deployment.</li><li>Supports 21 CFR Part 11 and GxP compliance for regulated workflows.</li><li>Integrates seamlessly with waters_connect, Empower, and MassLynx to optimize productivity.</li></ul><h5><strong>Who should attend?</strong></h5><p>If you work in Pharma or Biopharma as an IT Manager, R&amp;D Scientist, or QA/QC Scientist, this exclusive webinar is designed for you.</p><p><i><strong>Don't miss it.</strong></i></p><blockquote><p><strong>Presenter:</strong> Guillaume Mignard (OneLab Product Marketing Manager, Waters Corporation)</p><p>Guillaume Mignard is Product Designer and Product Owner of OneLab™ Software at Waters Corporation.</p><p>Since joining Waters in 2017, he has led the strategic direction, design, and implementation of OneLab™ Software, a cloud-based platform making lab automation accessible to scientists worldwide.</p><p>Guillaume began his career as a UX/UI designer for business software, pioneering user-centric design when it was still emerging beyond web marketing.</p></blockquote></div>

Waters Corporation: Introducing the Waters OneLab Secure Deployment Solution

Introducing the Waters OneLab Secure Deployment Solution

Join our exclusive webinar to discover how the Waters OneLab™ Secured Deployment Solution takes you from box to bench.

Introducing Waters OneLab Secure Deployment Solution

<div><div container-id="cq-colctrl-lt0" comp-id="A1"><div><p><strong>Take your Chromeleon Instrument Methods to the next level with this focused and practical session. This webinar is specifically designed for Thermo Scientific Chromeleon CDS users, who want to enhance their current skills and gain a better understanding of how to control instrument actions and apply dynamic sequence logic.</strong></p><h4><strong>Topics covered include:</strong></h4><ul><li><strong>Script editor overview:</strong> Understand the basics of writing and editing custom scripts</li><li><strong>Conditional statements:</strong> Learn how to use logic to make conditional decisions during runs and sequences</li><li><strong>Information logging:</strong> Record key instrument and method events in real time for extended audit trail coverage</li><li><strong>Custom sequence variables: </strong>Control sequence and instrument behavior and with user-defined fields to enrich meta data capture</li><li><strong>User-defined programs:</strong> Customize injection actions to support complex workflows</li><li><strong>Automated startup and shutdown: </strong>Create routines to prepare instruments for operation or safely power them down</li></ul><h4><strong>Why Attend:</strong></h4><p>Join this webinar to gain practical skills and expert tips for using Chromeleon CDS more effectively. Whether you’re new or experienced, you’ll learn how to streamline workflows and enhance your analytical instrument methods.</p><p><strong>Cannot attend the live broadcast?&nbsp;</strong></p><p><i>Please register anyway, and we will automatically send you the link to the recording.</i></p><blockquote><p><strong>Presenter: </strong>Peter Zipfell (Product Marketing Manager, Thermo Fisher Scientific)</p></blockquote></div></div></div>

Thermo Fisher Scientific: Get more from your Chromeleon Instrument Methods

Get more from your Chromeleon Instrument Methods

Join this webinar to gain practical skills and expert tips for using Chromeleon CDS more effectively.

<h3><strong>Screening Demystified: Practical Guidelines for Getting It Right with High-Resolution</strong></h3><p>Join us for an insightful two-part webinar series exploring high-resolution LC/MS screening and unlocking instrument capabilities.</p><p>In these sessions, we’ll address common misconceptions about HRMS screening and provide practical guidance to help you achieve confident, efficient screening in complex analytical workflows. Discover strategies, best practices, and expert insights that will empower you to streamline your processes and maximize the value of your instrumentation.</p><h4><strong>Part 1: All About Screening</strong></h4><p>Screening with LC/QTOF can bring a new dimension to many labs’ capabilities, massively expanding the scope of their analyses. However, although QTOF screening is a powerful tool, its complexity should not be underestimated; high resolution accurate mass spectrometry (HRAMS) data is inherently complex and careful experimental design and deployment of the correct hardware and software tools are vital to avoid potential pitfalls like false positives or negatives, poor reproducibility and possibly even regulatory or reputational risks for the lab itself. This session will challenge some of the misconceptions surrounding HRAMS screening and will introduce general concepts, such as targeted, suspect and non-targeted screening workflows.</p><h5><strong>Who should attend?</strong></h5><p>Scientists already using HRMS who need insights about their methods, results, or workflows and scientists considering moving to HRMS screening and looking for clarity on what it can and can’t deliver.</p><blockquote><p><strong>Presenter: </strong>Jonathan Spencer (Field Application Specialist LC/MS, Agilent Technologies)</p><p>Jonny studied BSc Natural Sciences at the University of Nottingham, where he divided his studies between chemistry and biochemistry. He went on to study MSc Forensic Science at Sheffield Hallam University. Following graduation, he spent 2 years as a Confirmatory Analyst in an anti-doping and forensic toxicology lab, before joining Agilent as an LC-MS Applications Scientist. At Agilent, he focuses on small molecule applications using LC-TQ and LC-QTOF in fields like food, forensic and environmental analysis.</p><p><strong>Presenter:&nbsp;</strong>Christian Hegmanns (Application Specialist LC/MS, Agilent Technologies, Inc.)</p><p>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.</p></blockquote>

Agilent Technologies: Screening Demystified: Practical Guidelines for Getting It Right with High-Resolution

Screening Demystified: Practical Guidelines for Getting It Right with High-Resolution Part 1: All About Screening

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