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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N-linked glycosylation is a critically important and complex post-translational modification.
The structure of N-linked glycans can influence the function of glycosylated biotherapeutics, making the characterization of N-glycans an essential part of the therapeutic development process.
In this The Lab Central Premiere, learn about Agilent&#39;s complete offering of glycan sample preparation and analysis consumables to support a comprehensive end-to-end N-glycan workflow solution.
<blockquote>
Presenter: Dr. Ashish Pargaonkar (Lead for Biopharma Workflow Commercialization, Agilent Technologies)
</blockquote>
<blockquote>
Presenter: Ms. Paramjeet Khandpur (Biopharma Workflow Commercialization Lead, Agilent Techologies)
</blockquote>

Agilent Technologies: The Glycan Connection

The Glycan Connection

Learn about Agilent's complete offering of glycan sample preparation and analysis consumables to support a comprehensive end-to-end N-glycan workflow solution.

Join us for our 3-Part series to Meet our Experts and discuss topics including:
<ul>
<li>History of HPLC column technology over the last 50 years and how advancements have helped address current separation challenges.
</li>
<li>Fundamentals of small molecule separations to enable you to develop methods more efficiently. 
</li>
<li>Solvent and column choices with UPLC to develop more environmentally friendly chromatography methods
</li>
</ul>
<h4>PART 3: Achieving Your Sustainability Goals with UPLC</h4>
Method development for reversed-phase high-performance liquid chromatography (HPLC) separations has traditionally been conducted using acetonitrile-water or methanol-water gradients. Acetonitrile is often preferred because of its ability to dissolve a wide range of solutes, its low UV cutoff, compatibility with mass spectrometry detection, and lower viscosity. However, its use can also be problematic due to health and environmental concerns. This presentation will highlight how to reduce the use of acetonitrile while maintaining separation performance by using narrower ID columns containing smaller particles. Chromatography using alternatives to acetonitrile such as isopropanol or ethanol will be shown utilizing high-pressure LC instrumentation. Both techniques could be employed when developing more environmentally friendly LC methods.
<blockquote>
Presenter: Bonnie Alden (Principal Scientist, Research &amp; Development, Waters Corporation)
</blockquote>
<blockquote>
Bonnie Alden joined Waters Corporation in 1982 to work with Dr. Patrick McDonald to develop new Sep-Pak Cartridge SPE devices. During her career, she has been a member of teams that brought transformative chromatographic columns to market. These include Symmetry Columns which set the industry standard in reproducibility, 1st hybrid chromatographic packing of XTerra Columns, 2nd generation Ethylene Bridged Hybrid (BEH) and Charged Surface Hybrid (CSH) technologies, as well as the recent development of modern, mixed-mode stationary phases for challenging analyses, such as the retention and separation of polar acids. More than 35 years later, she is still an enthusiastic student of liquid chromatography and separation science. Bonnie is currently a principal scientist in the Small Molecule Portfolio Team where her research interests have focused on developing products to address the needs of scientists in the extensive field of small molecule drug development.
</blockquote>

Waters Corporation: Achieving Your Sustainability Goals with UPLC

Achieving Your Sustainability Goals with UPLC

How to reduce the use of acetonitrile while maintaining separation performance by using narrower ID columns containing smaller particles.

The development and expansion of analytical methods for per- and polyfluoroalkyl substances (PFAS) in food is essential for the continued monitoring of the United States (US) food supply and assessments of dietary intake.
In March of 2022, the European Union Reference Laboratory (EURL) for halogenated persistent organic pollutants (POPs) in Feed and Food released a guidance document covering priority PFAS of interest, including analytical method parameters and limits of quantification (LOQs). As a result, the Food and Drug Administration (FDA) began method extension work to incorporate ten new additional analytes to method C-010.02 including long chain perfluorosulfonic acids, fluorotelomer sulfonates, and perfluorooctane sulfonamide. In December of 2022, The European Union published Commission Regulation 2022/2388, establishing maximum levels for perfluorooctane sulfonic acid (PFOS), perfluorooctanoic acid (PFOA), perfluorononanoic acid (PFNA), and perfluorohexane sulfonic acid (PFHxS) in certain foodstuffs, primarily fish, molluscs, crustaceans, and eggs. As a result, the FDA method was evaluated for performance in reaching EU required LOQs for both compliance and monitoring purposes. The FDA method was found to be able to reach all required LOQs for analytes in matrices with established maximum levels and with further method modifications, required LOQs could be met in fruits, vegetables, and milk.
Key Learning Points:
<ul>
<li>Understand the FDA’s approach for PFAS LOQs in various food matrices
</li>
<li>Learn about the EU reference lab guidance for PFAS in foods and how the FDA is taking a similar approach to food safety
</li>
<li>Take a deep dive into which PFAS are designated targets and which are being monitored for screening
</li>
</ul>
Who Should Attend:
<ul>
<li>Any scientists, lab analysts, food safety advocates, food manufacturers or anyone interested in food safety.</li>
</ul>
<blockquote>
Presenter: Susan Genualdi Ph.D. (Research Chemist, Food and Drug Administration)
</blockquote>
<blockquote>
Susan Genualdi is currently a Research Chemist in the Center for Food Safety and Applied Nutrition at the Food and Drug Administration. Her research over the last 12 years has focused on developing methods for the analysis of direct and indirect food additives in food and food packaging and for the last 6 years has focused on PFAS analysis in foods. Prior to her work at the FDA, she received her PhD in Analytical Chemistry at Oregon State University and was a postdoctoral fellow at Environment Canada.
</blockquote>
<blockquote>
Presenter: Richard F. Jack Ph.D. (Global Market Development Manager, Phenomenex)
</blockquote>
<blockquote>
Richard F. Jack, Ph.D. Richard is the Global Market Development manager for the environmental and food markets at Phenomenex corporation. He has over 18 yrs. experience with chromatography and mass spectrometry for the environmental, semiconductor, chemical, and pharmaceutical industries. Richard is a former EPA Scientific Advisor for the EPA’s panel on Hydraulic Fracturing, a coauthor for EPA 557 and 557.1 along with ASTM D8001 and updates to D4327 and D6919 methods. He is currently the Second Vice Chairman for the ASTM D19 subcommittee on water analysis. Richard received his Ph.D. in biochemistry and anaerobic microbiology from Virginia Tech University and Master’s in ecology from the University of Tennessee.
</blockquote>

Phenomenex: FDA’s Analytical Method for PFAS Detection

FDA’s Analytical Method for PFAS Detection

Understand the FDA’s approach for PFAS LOQs in various food matrices.

Key Learning Points:
<ul>
<li>Learn about types of tubing and fittings and making the best connections.
</li>
<li>Make sense of how to select the correct tube, properly cutting it and choosing the right fitting. 
</li>
<li>Understanding extra-column volume and what are Zero-Dead Volume connections.
</li>
<li>Tips and tricks to diagnose and troubleshoot poor tubing and/or fitting choices.
</li>
</ul>
Who Should Attend:
<ul>
<li>Any LC users wanting to deepen their knowledge of LC tubing and connections, including troubleshooting, to smoothly run their LC experiments</li>
</ul>
<blockquote>
Presenter: Lucia Geis Asteggiante (Senior Technical Specialist, Phenomenex)
</blockquote>
<blockquote>
Lucia is a Senior Technical Specialist that has recently joined Phenomenex’s Global Technical Team. She has a broad experience in the field of Analytical Chemistry with a particular focus on LC chromatography coupled with mass spectrometry. Lucia comes from a strong academic and regulatory background with experiences ranging from method development and analysis of small molecules to large protein complexes. She gained her Ph.D. at the University of Maryland - College Park, USA and did her post-doctoral work at the University of Oxford, UK. During her time as a researcher, she has authored/co-authored 23 scientific publications and 2 book chapters.
</blockquote>

Phenomenex: Spooktacular Solutions for LC Tubing and Connections

Spooktacular Solutions for LC Tubing and Connections

Learn about types of tubing and fittings and making the best connections.

Low-flow chromatography is ideal when samples are limited, when enhanced sensitivity and high resolution are needed, and compatibility with certain detectors/instruments are required.
Choosing the appropriate low-flow column is critical to the success of any proteomic analysis. The diverse portfolio of Thermo Fisher Scienitific columns offers uncompromised performance with an easy-to-use format for nano and capillary LC-MS analysis. Achieving state-of-the-art performance from nano-flow LS-MS has never been easier.
In this webinar, we will present the Thermo Scientific low-flow chromatography (capLC/NanoLC) columns and demonstrate how they are specifically designed to push nanoLC separations further. Learn how deeper proteomic coverage is achieved with the Thermo Scientific integrated column-emitter setup (EASY-Spray) and innovative Thermo Scientific micro-pillar array column (µPAC) technology.
<blockquote>
Presenter: Robert van Ling (Product Manager, Thermo Fisher Scientific)
</blockquote>
<blockquote>
Robert van Ling has 20+ years of experience in nanoLC separations for proteomics LC-MS. In previous roles, he has participated in the introduction in a variety of low-flow products, like the Thermo Scientific™ UltiMate™ 3000 Systems and Thermo Scientific™ PepMap™ and EASY-Spray™ Columns. In the last few years, Robert has focused his activities on the development and commercialization of µPAC HPLC columns, and is keen to share his experience.
</blockquote>
<blockquote>
Presenter: Jeff Op de Beeck (Staff Scientist, Research &amp; Development, Thermo Fisher Scientific)
</blockquote>
<blockquote>
Dr. Jeff Op de Beeck is currently Staff Scientist at Thermo Fisher Scientific’s R&amp;D facility in Ghent where micro pillar array technology is developed and produced. His work under supervision of Prof. Gert De Smet and Prof. Wim De Malsche formed the basis for the current micro Pillar Array Column, which is branded by Thermo Fisher Scientific as the micro-Pillar Array Column (µPAC™). He holds a master’s degree in Biomedical Sciences from the University of Antwerp and a Ph.D. in Chemical Engineering from the University of Brussels.
</blockquote>

Thermo Scientific: Push low-flow separations for LC-MS proteomic workflows further with integrated column-emitter and innovative micro-pillar array column (µPAC) technology

Push low-flow separations for LC-MS proteomic workflows further with integrated column-emitter and innovative micro-pillar array column (µPAC) technology

Thermo Scientific low-flow chromatography (capLC/NanoLC) columns and demonstrate how they are specifically designed to push nanoLC separations further.

Push low-flow separations for LC-MS proteomic workflows

Per- and polyfluoroalkyl substances (PFAS) have been a hot topic for the past few years, and substances of interest for decades.
Recently, the European Food Safety Authority (EFSA) established tolerable weekly intakes for four PFAS substances, leading to maximum limits within the European Union for these compounds in fish, meat, and eggs. This development means that robust and sensitive analytical methods for PFASs are in high demand.
Wageningen Food Safety Research (WFSR) has developed several methods to serve the different purposes of PFAS analysis: official food control, monitoring at low levels for risk assessments, and research into additional substances and matrices. In this webinar, Dr. Kerstin Krätschmer and Dr. Richard Jack will give an overview of the methods, common challenges, the validation scheme described in the guidance document published by the European Union Reference Laboratory (EURL) for POPs in feed and food, and some analysis results in food and produce from the Netherlands.
Key learning objectives
<ul>
<li>Learn about PFAS sample preparation and analysis challenges from food matrices
</li>
<li>Understand how to ensure performance requirements for European Reference Laboratory requirements
</li>
</ul>
Who should attend?
<ul>
<li>Scientists and lab technicians involved in PFAS analysis
</li>
<li>Food safety analysts
</li>
<li>Food manufacturers that wish to learn more about PFAS analysis
</li>
</ul>
<blockquote>
Presenter: Kerstin Krätschmer, PhD (Wageningen Food Safety Research)
</blockquote>
<blockquote>
Dr. Kerstin Krätschmer is a state examined food chemist who studied food chemistry (MSc) at Bergische Universität Wuppertal, Germany and completed legal training at the State Institute for Chemical and Veterinary Analysis Krefeld (CVUA-RRW) and the Consumer Protection Authority Düsseldorf. After finishing her PhD at the European Union Reference Laboratory for halogenated Persistent Organic Pollutants (POPs) in Freiburg and University of Hohenheim in Stuttgart, Germany, she became project leader of the National Reference Laboratory for halogenated POPs of the Netherlands at Wageningen Food Safety Research. Her main focus lies on POPs in food and feed, but also includes potential food safety risks within the circular economy.
</blockquote>
<blockquote>
Presenter: Dr. Richard Jack (Phenomenex, Inc.)
</blockquote>
<blockquote>
Dr. Richard Jack is the Global Market Development manager for the environmental and food markets at Phenomenex corporation. He has over 18 years’ experience with chromatography and mass spectrometry for the environmental, semiconductor, chemical, and pharmaceutical industries. He is a former EPA Scientific Advisor for the EPA’s panel on Hydraulic Fracturing, a coauthor for EPA 557 and 557.1 along with ASTM D8001 and updates to D4327 and D6919 methods. He is currently the Second Vice Chairman for the ASTM D19 subcommittee on water analysis. He received his PhD in biochemistry and anaerobic microbiology from Virginia Tech University, USA and he has a Master’s in ecology from the University of Tennessee.
</blockquote>
<blockquote>
Presenter: Ellen Simms (Assistant Editor, SelectScienc)
</blockquote>
<blockquote>
Ellen studied biological sciences at the University of the West of England, UK, before completing a master&#39;s in epidemiology from the University of Bristol. As a member of the Editorial team, she now plays an integral role in shaping the content on SelectScience.
</blockquote>

SelectScience: Strategies to address monitoring and compliance testing of PFAS in food

Strategies to address monitoring and compliance testing of PFAS in food

Overview of the methods, common challenges, the validation scheme described in the guidance document published by the European Union Reference Laboratory.

Strategies to address monitoring and compliance testing

In less than twenty minutes we are going to show you how you can speed up method development by 30 % AND increase your assay precision 10-fold.
If you have ever:
<ul>
<li>had to troubleshoot poor peak shape</li>
<li>suffered from irreproducible results</li>
<li>lacked the resolution you need</li>
</ul>
Then this webinar is for you.
Our latest family of columns have been designed for out-of-the-box performance, maximizing your chance of getting it right first time. We have done this by packing our most reproducible and stable particles into new, high-performance hardware, which mitigates many of the challenges you currently face, whilst still providing the selectivity you are used to. These columns are available for both UHPLC and HPLC systems. A major pharmaceutical company recently described these columns as a &quot;non-negotiable&quot; part of their workflow.
<blockquote>
Presenter: Hazel Dickson (Market Development Manager Europe, Waters Corporation)
</blockquote>

Waters Corporation: Speed up HPLC method development by 30 %

Speed up HPLC method development by 30 %

How you can speed up method development by 30 % AND increase your assay precision 10-fold.

Metabolomics refers to the comprehensive measurement of small molecules in biofluids by either mass spectrometry (MS) or nuclear magnetic resonance (NMR) with the aim of covering multiple KEGG (Kyoto Encyclopedia of Genes and Genomes) pathways, exposome products, and chemical reactions to provide new insights into disease etiologies.
Lipidomics is a subset of metabolomics focused specifically on the analysis of lipid species. MS-based metabolomics and lipidomics generally require the use of liquid chromatography to separate metabolites based on polarity and high-resolution MS to accurately measure the mass-to-charge (m/z). The combination of retention time and m/z accuracy provides a reliable method to identify metabolites, which is critical for making disease marker discoveries.
In this webinar, Dr. Timothy Garrett, associate professor at the University of Florida, will discuss the clinical translation of metabolomics using examples of different diseases including rare diseases, cancer, and infectious diseases. He will explain how critical chromatography is to reproducibility and metabolite identification, and how new monodisperse columns can aid in separation and identification.
Key learning objectives
<ul>
<li>Learn the basics of applied metabolomics using UHPLC-HRMS/MS
</li>
<li>Understand how metabolomics can be used for developing new diagnostic tests
</li>
<li>Understand the potential of metabolomics and the current limitations
</li>
<li>Explore the role of chromatography in metabolomics
</li>
<li>Learn how utilizing monodisperse fully porous particles can improve your current metabolomics method
</li>
</ul>
Who should attend?
<ul>
<li>LC scientists looking for more efficiency for their metabolomic separations
</li>
<li>Scientists looking to improve their current HPLC/UHPLC separations for metabolomics
</li>
<li>Chromatographers looking to start developing new metabolomics based HPLC/UHPLC based methods
</li>
</ul>
<blockquote>
Presenter: Timothy J. Garrett (Associate Professor, University of Florida)
</blockquote>
<blockquote>
Dr. Timothy Garrett is an Associate Professor and Chief of Experimental Pathology in the Department of Pathology, Immunology and Laboratory Medicine at the College of Medicine at The University of Florida. He received his undergraduate degree from the University of Georgia in Chemistry and his PHD in Chemistry from the University of Florida. He joined the University of Florida in 2006, where he has developed a research program in metabolomics, lipidomics, and small molecule quantitation for clinical and biological research using mass spectrometry approaches. He is also currently Co-Editor-in-Chief for the Journal of Mass Spectrometry and Advances in the Clinical lab.
</blockquote>
<blockquote>
Presenter: Carrie Haslam (SelectScience)
</blockquote>
<blockquote>
Dr. Carrie Haslam is an Associate Editor at SelectScience, playing a key role in content production and specializing in Materials Science, Alzheimer’s disease and Clinical Diagnostics. Carrie completed a Ph.D. from The University of Plymouth, where she developed graphene-based biosensors for the early diagnosis of Alzheimer’s disease.
</blockquote>

SelectScience: The role of chromatography and monodisperse particles in mass spectrometry-based metabolomics for disease detection

The role of chromatography and monodisperse particles in mass spectrometry-based metabolomics for disease detection

The clinical translation of metabolomics using examples of different diseases including rare diseases, cancer, and infectious diseases.

Chromatography and monodisperse particles in MS metabolomics

Oligonucleotide analysis is a critical aspect of molecular biology and therapeutic development, demanding robust and versatile chromatographic techniques for comprehensive characterization.
Several modes of chromatography can be employed to characterize these biomolecules, but when and how to best use each mode can be challenging.
This webinar aims to explore how various chromatographic techniques can be synergistically employed to achieve comprehensive oligonucleotide characterization. Aspects of ion-pair reversed phase chromatography (IP-RPC), hydrophilic interaction liquid chromatography (HILIC), ion exchange chromatography (IEC), and size exclusion chromatography (SEC) will be discussed and how best to employ each mode in oligonucleotide characterization. Several application examples will be utilized to showcase how each of these modes of chromatography can be best utilized to fully resolve and understand the composition of samples containing oligonucleotides.
At the conclusion of the webinar, the audience member will:
<ul>
<li>Understand the strengths and weaknesses of each mode of chromatography in characterizing oligonucleotides.
</li>
<li>Be familiar with key method parameters to adjust when fine-tuning oligonucleotide chromatographic assays
</li>
<li>Gain an appreciation for when to use each mode of chromatography when analyzing oligonucleotides
</li>
</ul>
<blockquote>
Presenter: Cory E. Muraco (Biomolecule Workflows Manager, Merck KGaA, Darmstadt, Germany)
</blockquote>
<blockquote>
Cory joined the company in 2013, starting in the Chemical Standards division, developing and validating analytical methods for testing the purity of certified reference materials using GC and LC methods. In 2022, Cory assumed his present role, where he is tasked with supporting the design, development, and execution of the marketing and R&amp;D strategies around bioanalytical strategy.
</blockquote>
<blockquote>
Presenter: Andrea Krumm (Product Manager, Analytical Columns, Tosoh Bioscience GmbH)
</blockquote>
<blockquote>
Andrea Krumm studied biotechnology before gaining a PhD in Cell and Cancer Biology. After four years as an applications specialist for optical analytical devices used in academic and pharmaceutical research, she joined Tosoh Bioscience GmbH in 2020 as a product manager for analytical columns. Andrea is responsible for gathering customer requirements, application areas and addressing these with new and existing products of the analytical columns line.
</blockquote>

Merck: Exploring Oligonucleotide Diversity: Insights From Multiple Modes of Chromatography

Exploring Oligonucleotide Diversity: Insights From Multiple Modes of Chromatography

How various chromatographic techniques can be synergistically employed to achieve comprehensive oligonucleotide characterization.

Oligonucleotide Diversity: Multiple Modes of Chromatography

The recent success of mRNA vaccines demonstrates the capabilities of nucleic acid-based drugs. These new modalities hold the promise of delivering not only potent vaccines, but also enzyme replacement therapies. However, there is a need for more analytical characterization tools to provide more informationon stability, heterogeneity, drug design and structure-function relationships. Anion-exchange (AEX) and size exclusion (SEC) chromatography techniques are well suited to providing high resolution separations of nucleic acids and their carriers.
AEX and SEC offer comprehensive quality and impurity profiling, but have suffered with previous methods from unsatisfactory recovery and resolution, poor MS compatibility. In addition, column hardware and packing materials have exhibited problematic secondary interactions. We have explored alternative mobile phase conditions in combination with various packing materials and sorbents in parallel with using novel low adsorption hardware allowing for more robust platform method for multiple drug substances and sample types, including AAVs and mRNA.
Learning Objectives Include:
<ul>
<li>Comprehensive overview of both theoretical and practical aspects of modern AEX and SEC separations.
</li>
<li>New solutions and method parameter consideration for design of robust methods for nucleic acid separations.
</li>
<li>Chromatography examples for small to very large nucleic acids
</li>
</ul>
<blockquote>
Presenter: Szabolcs Fekete PhD (R&amp;D Investigator, Waters Corporation)
</blockquote>
<blockquote>
Dr. Szabolcs Fekete worked as an analytical R&amp;D scientist in the pharmaceutical industry for 10 years then moved to the University of Geneva and worked as a scientific collaborator for a decade. In April 2021, he joined Waters Corporation and now works as one of the Chemistry department’s lead application and development scientists. . He has contributed to 200 pieces of published work.
</blockquote>

Waters Corporation: New Insights on Anion Exchange and Size Exclusion of Nucleic Acids

New Insights on Anion Exchange and Size Exclusion of Nucleic Acids

We have explored alternative mobile phase conditions in combination with various packing materials and sorbents.

LCMS webinars focusing on Consumables - page 14