<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

Article

Webinars

Video

Scientists

Scientific article

Interview

Science and research

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

LabRulez

Organomation, founded in 1959, designs and manufactures high-quality nitrogen evaporators and extraction systems. Known for innovation and durability, their lab instruments are used globally for efficient sample preparation with strong customer support.

Organomation

Agilent Technologies

Technology Networks

Unchained Labs

Phenomenex

SelectScience

C&EN

SCIEX

Evosep Biosystems

<p><strong>Biological samples represent formidable challenges in sample preparation that hold important consequences for LC analysis. Cleaner samples translate to more robust, reproducible LC analysis, with fewer repeat runs, and less equipment down time. The challenge is knowing which sample preparation technique to combine with both your sample and LC method.</strong></p>
<p>In this discussion we will look at some common bio sample preparation techniques, from solvent exchanges to solid phase extractions. We will then discuss how to match the sample preparation technique to both your sample and the desired outcome of your chromatography.</p>
<blockquote>
<p><strong>Presenter:</strong> Melissa Goodlad (Application Engineer, Agilent Technologies, Inc.)</p>
</blockquote>
<blockquote>
<p>Melissa Goodlad is an Application Engineer providing applications assistance and technical support for Agilent’s HPLC columns and consumables. Before joining Agilent, Melissa was completing her PhD in Physical Chemistry at UC Merced studying nanoparticle self-assemblies.</p>
</blockquote>


Agilent Technologies: Sample Preparation for Improved LC Bio Separations

Sample Preparation for Improved LC Bio Separations

In this discussion we will look at some common bio sample preparation techniques, from solvent exchanges to solid phase extractions.

<p><strong>If you are new to our technology or just getting started this event is for you. We will introduce the basics of the Evosep One technology and include hot-from-the-lab data from our users. Nicolai Bache, Head of Applications at Evosep, will host the event, bringing you up to speed with the latest additions to the Evosep One technology.</strong></p>
<p>The Evosep One is a plug-and-play standardized platform designed for robustness and high throughput. It has been designed specifically to address and eliminate the prevalent challenges associated with throughput and robustness of nano-flow LC-MS workflows while maintaining sufficient sensitivity and resolving power for clinical applications.</p>
<p>The Evosep One technology is centered around the Evotip and integrates sample preparation with LC-MS. The Evotip is essentially a disposable trap column in a pipette tip format with a small plug of C18 stationary phase at the bottom of the tip. The Evotips are used to desalt and clean up the samples prior to LC-MS analysis, however, the traditional subsequent steps of eluting, drying down, re-suspending the samples from tips are completely omitted and instead the tips are loaded directly into Evosep One for analysis.</p>
<p>The system uses four low-pressure syringe pumps in parallel to elute samples from the Evotip with a chromatographic gradient. The resulting gradient with the pre-separated sample is moved into a storage loop, that is then switched in-line with a single high-pressure pump and an analytical separation column for focusing. With this simplified workflow on pre-set gradients, the Evosep One offers a throughput from 30 to 300 samples per day.</p>
<h5><strong>1. A beginner’s guide to the Evosep One</strong></h5>
<ul>
<li>Presenter: Nicolai Bache (Head of applications at Evosep)</li>
</ul>
<p>The Evosep One technology is centered around the Evotip and integrates sample preparation with LC-MS. The Evotip is essentially a disposable trap column in a pipette tip format with a small plug of C18 stationary phase at the bottom of the tip. The Evotips are used to desalt and clean up the samples prior to LC-MS analysis, however, the traditional subsequent steps of eluting, drying down, re-suspending the samples from tips are completely omitted and instead the tips are loaded directly into Evosep One for analysis.</p>
<h5><strong>2. To be announced</strong></h5>
<ul>
<li>Presenter: Anh Reynolds (Associate Scientist at BMS)</li>
</ul>
<h5><strong>3. Clinical proteomics in the fast lane – Combination of robust LC, timsTOF based IMS-MS and GPU powered data processing</strong></h5>
<ul>
<li>Presenter: Allan Stensballe (Industrial PHD at Aalborg University)</li>
</ul>
<p>Mass spectrometrists who have been in the proteomics field long enough to be users of both early gel-free and gel-based strategies have learned to appreciate robust and fast analysis pipelines. As clinical proteomics projects now increasingly moves towards larger cohort studies and integration in multiOmics projects the stability and reproducibility of LC-MS to data analysis is imperative.  In this talk I will highlight our experiences, project examples and thoughts on use of clinically optimized and standardized workflows.</p>


A beginner’s guide to Evosep

The Evosep One is a plug-and-play standardized platform designed for robustness and high throughput.

<h5><strong>Key Learning Points</strong></h5>
<ul>
<li><p>An overview of sample preparation strategies for synthetic oligonucleotides, including how to adjust experimental design depending on the oligo and sample matrix.</p>
</li>
<li><p>Find ways ensure effective sample preparation and cleanup methods are implemented.</p>
</li>
<li><p>Learn about method optimization for small volume sample extraction and clean-up solutions for oligonucleotides will be explored to further optimize challenging methods.</p>
</li>
</ul>
<h5><strong>Who Should Attend</strong></h5>
<p>Any Bioanalytical chemists new to working with oligonucleotides, or anyone new to oligonucleotide characterization by LC-MS</p>


Phenomenex: Novel Oligonucleotide Sample Clean-up and Method Optimizations

Novel Oligonucleotide Sample Clean-up and Method Optimizations

Sample preparation strategies for synthetic oligonucleotides, including how to adjust experimental design depending on the oligo and sample matrix.

Oligonucleotide Sample Clean-up and Method Optimizations

<p><strong>The lack of standardization and throughput in proteomics sample preparation has caused limitations within the field. Indeed, according to published reports, sample preparation traditionally accounted for 75% of the overall variability.</strong></p>
<p>Automating the universal ProtiFi S-Trap™ proteomics sample preparation system with the Tecan Resolvex® A200 directly addresses this issue to yield a standardized, high-throughput proteomics workflow suitable for preparing all samples reproducibly, including samples that may contain additional contaminants such as surfactants in bioreactor supernatants.</p>
<p>In this webinar, Dr. John P. Wilson, Ph.D. and Dr. John D. Laycock, Ph.D., will share how to use the affordable, small-footprint A200 and S-Trap™ 96-well plates to quickly and easily prepare samples for proteomics analysis without further method development.</p>
<p>Join this free expert webinar to learn:</p>
<ul>
<li><strong>What the Tecan Resolvex®A200 is, how it operates, and how easy it is to use</strong></li>
<li><strong>The traditional difficulties and importance of reproducible sample preparation</strong></li>
<li><strong>How the combination of the A200 and the S-Trap™ sample preparation system affords a standardized, universal system that provides high reproducibility and throughput at low cost without change of protocol</strong></li>
</ul>
<p>Who should attend:</p>
<ul>
<li>All scientists and end users, regardless of skill level, who are in or wish to conduct proteomic sample preparation</li>
<li>All scientists and end users who use the multi-attribute method (MAM) in the development, quality control, and production of biological drugs</li>
<li>All scientists and end users who seek a standardized solution to the difficulties in proteomics sample preparation</li>
</ul>
<blockquote>
<p><strong>Presenter:</strong> Dr. John P. Wilson (Founder and CEO, ProtiFi)</p>
</blockquote>
<blockquote>
<p>Dr. John P. Wilson, Ph.D., is Founder and CEO of ProtiFi, an omics-solutions innovator with the goal to bring precision omics to life™, originally spun out of Cold Spring Harbor Laboratory (CSHL). Dr. Wilson has dedicated his career to developing new transformative technologies to increase the speed, robustness, and reproducibility of omics analyses. Technologies include the S-Trap and Si-Trap sample preparation systems, the engineered Tryp-N enzyme, and SimpliFi, ProtiFi&#39;s cloud-based, intuitive omics analysis platform. He received his Ph.D. from the Rockefeller University and postdoced at CSHL with Prof. Dr. Darryl J.C. Pappin, a founder of the field of proteomics.</p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Dr. John D. Laycock (Director of Technology and Product Development, Tecan SP)</p>
</blockquote>
<blockquote>
<p>John D. Laycock is the Director of Technology and Product Development at Tecan SP in Baldwin Park, CA. He attended the University of Florida and completed a dissertation in the area of tandem mass spectrometry of porphyrins and received a PhD in 1994. He joined the Center of Human Toxicology in 1995 as a Postdoctoral Associate responsible for introducing LC-MSMS methodologies to the lab utilizing GC-MS as the primary bioanalytical tool. He joined Amgen in Thousand Oaks, CA in 1998 where he was responsible for setup of the first small molecule GLP bioanalytical lab there. While at Amgen, he implemented laboratory automation, LIMS, and informatics to holistically streamline workflows for bioanalytical sample analysis and reporting throughout all stages of drug development. In 2015 he joined SPEware which was acquired by Tecan in 2016..With Tecan he has been responsible for launch of the Resolvex A200 and various chemistry consumable products into the global marketplace.</p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Ellen Simms (Assistant Editor, SelectScience)</p>
</blockquote>
<blockquote>
<p>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.</p>
</blockquote>


SelectScience: Automated proteomics sample prep: Realizing the need for higher throughput, robustness, and standardization

Automated proteomics sample prep: Realizing the need for higher throughput, robustness, and standardization

How to use A200 and S-Trap 96-well plates to quickly and easily prepare samples for proteomics analysis without further method development.

Automated proteomics sample prep: High throughput ...

<p><strong>Tissue homogenization and cell lysis are crucial steps in protein extraction for LC-MS-based proteomics and many other research applications.</strong></p>
<p>During this webinar, you will discover ways to improve your protein extraction, such as by reducing workflow complexity, improving results from scarce samples, setting up robust assays and working with large sample cohorts. But why stop here?</p>
<p>We will also show how the full sample preparation workflow for LC-MS-based proteomics can be standardized and simplified with the BeatBox platform, which was developed for a wide variety of sample matrices and input ranges as well as how this can be applied to research such as cancer biomarker identification.</p>
<p>Attend this webinar to:</p>
<ul>
<li>Learn how to obtain reliable results through reproducible sample homogenization, even for challenging proteomics projects</li>
<li>Explore how to simplify and standardize the full sample preparation workflow for LC-MS-based proteomics</li>
<li>Discover how the BeatBox, a novel tissue homogenizer and cell lyser, can help you to efficiently extract proteins from a wide range of tissue and cell types</li>
</ul>
<blockquote>
<p><strong>Presenter:</strong> Jasmin Johansson (Application Scientist, PreOmics)</p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Dr. Silvia Wuertenberger (Product Manager, PreOmics)</p>
</blockquote>


Technology Networks: Streamlining Protein Extraction for Proteomics and Beyond

Streamlining Protein Extraction for Proteomics and Beyond

You will discover ways to improve your protein extraction, such as by reducing workflow complexity, improving results from scarce samples ...

<p>Key learning objectives</p>
<ul>
<li><p><strong>Reversed Phase-Ion Pair LC for Oligos - Challenges and Optimization</strong></p>
</li>
<li><p><strong>Rapid Isolation of Oligo Therapeutics from Biological Samples</strong></p>
</li>
<li><p><strong>High-throughput, RPC Purification</strong></p>
</li>
</ul>
<blockquote>
<p><strong>Presenter:</strong> Mahesh Thondawada (Business Development Manager Biopharma/Biologic)</p>
</blockquote>


Analytical BioSolutions for Therapeutic Oligonucleotides

Reversed Phase-Ion Pair LC for Oligos - Challenges and Optimization...

<p><strong>Sepsis is a growing global challenge due to factors such as high mortality rate and the increasing prevalence of antimicrobial resistance.</strong></p>
<h4><strong>A single and rapid Zeno SWATH DIA proteomic analysis for concomitant identification and antibiotic resistance profiling of micro-organisms from positive blood cultures</strong></h4>
<ul>
<li><strong>Presenter:</strong> Iulia MACAVEI, PhD (student in Analytical Chemistry, Biological Analysis and Mass Spectrometry, University of lyon)</li>
</ul>
<p>Today, approximately 1.3 million people die each year worldwide from bacterial antimicrobial resistance (AMR). AMR is of great concern in the context of bloodstream infections (BSIs) when it evolves into sepsis. If MALDI-TOF has markedly shortened the delay of the pathogen identification step, AMR evaluation is still based on growth tests in the presence of antibiotics. With the aim of streamlining this turnaround time to less than 90min from a positive blood culture, the LC/Zeno SWATH DIA sensitivity and specificity performances were evaluated to concomitantly provide the identity and antibiotic resistance profile of etiological agents related to BSIs based on peptide surrogates.</p>
<h4><strong>Plasma proteomic landscape and patient heterogeneity in sepsis revealed by high-throughput mass spectrometry</strong></h4>
<ul>
<li><strong>Presenter:</strong> Dr. Yuxin Mi (Researcher at Wellcome Centre for Human Genetics, University of Oxford)</li>
</ul>
<p>Incomplete knowledge of the sepsis plasma proteome has limited our understanding of pathophysiology in the heterogeneous syndrome of sepsis. Here we apply high-throughput liquid chromatography – tandem mass spectrometry to delineate the plasma proteome for sepsis and comparator groups, involving 2622 samples in a single batch. We show how this scale of data can establish shared and specific proteins, pathways and co-expression modules in sepsis, and be integrated with paired leukocyte transcriptomic data. This work reveals novel subphenotypes informative for the response state and differential outcome, highlighting opportunities for a systems-based precision medicine approach to sepsis.</p>


SEPSIS

In this webinar we will uncover how our users combine technology with the Evosep One to further research into sepsis and its biomarkers.

Evosep SEPSIS

<p><strong>Get insight into topics ranging from the history of PFAS to analytical testing methods.</strong></p>
<p><strong>Day 1:</strong> Participate in an open discussion forum with our internal PFAS scientists from across the globe. Hear the story of how PFAS has shaped our environmental research. Take advantage of this digital space to share, learn and teach your fellow colleagues in the PFAS testing world.</p>
<p>Join this event to:</p>
<ul>
<li><strong>Learn about the history of PFAS and the need to increase testing for these “forever chemicals”</strong></li>
<li><strong>Understand how PFAS regulations differ across the globe</strong></li>
<li><strong>See what the future could look like in the PFAS testing world</strong></li>
<li><strong>Explore different matrices for PFAS testing</strong></li>
<li><strong>Discover how LC-MS can help solve challenges related to testing for PFAS chemicals</strong></li>
<li><strong>Get tips and tricks from seasoned PFAS testing experts</strong></li>
<li><strong>Find out what your peers are doing and share your knowledge in our open forum</strong></li>
</ul>
<p>This 2-day event is the first session of many PFAS summits SCIEX will host in the coming year, and there will be exciting activities for you to participate in throughout 2023. Join us for this first session and find out more about the next one: the in-person version!</p>
<h3><strong>Agenda Day 1</strong></h3>
<h5><strong>A brief history of PFAS</strong></h5>
<ul>
<li><strong>Dr. Craig Butt</strong> (Manager, Applied Market, SCIEX)</li>
</ul>
<h5><strong>Part 1: PFAS workflow overview: past, present and future</strong></h5>
<h5><strong>Part 2: The EMEAI perspective</strong></h5>
<ul>
<li><strong>Simon Roberts</strong> (Staff Application Scientist, SCIEX)</li>
<li><strong>Jianru Stahl-Zeng</strong> (Senior Technical Manager, EMEAI, SCIEX)</li>
</ul>
<h5><strong>PHX complementary workflow</strong></h5>
<ul>
<li><strong>Sam Lodge</strong> (Senior Business Development Manager, Phenomenex)</li>
</ul>
<h5><strong>Automating the Solid Phase Extraction (SPE) of PFAS for a range of methods and matrices</strong></h5>
<ul>
<li><strong>Ian Wan</strong> (Product Manager, PromoChrom Technologies)</li>
</ul>
<h5><strong>What does 4ppq actually look like?</strong></h5>
<ul>
<li><strong>Karl Oetjen</strong> (Senior Scientist, Technical Marketing, SCIEX)</li>
</ul>
<h5><strong>PFAS and customer support overview</strong></h5>
<ul>
<li><strong>Megumi Shimizu</strong> (LC-MS Application Scientist, SCIEX)</li>
</ul>
<h5><strong>An overview of different PFAS exposure pathways</strong></h5>
<ul>
<li><strong>Holly Lee</strong> (Food LC-MS Scientist, SCIEX)</li>
</ul>


PFAS summit: a scientific series (Day 1)

Join the discussion as SCIEX customers and industry experts explore how forever chemicals have shaped our environmental research.

<p><strong>The AssayMAP Bravo is a flexible yet easy-to-use automated micro chromatography-based protein sample preparation platform that leverages packed resin bed cartridges, precision flow control, and preoptimized applications to perform a wide variety of sample preparation workflows required during biotherapeutic development.  We have made several advances that allow the AssayMAP Bravo to address even more of the drug development process.  The system can now use large capacity cartridges, work in 21 CFR part 11 compliant labs, and automatically generate reports detailing the sample preparation steps executed.  These new capabilities enable walkup operation, simplified documentation, and seamless method transfer between labs so projects can be moved forward as quickly as possible.</strong></p>
<p>Key Learning Objectives:</p>
<ul>
<li>Discover how the AssayMAP Bravo makes automated sample preparation accessible to non-automation experts to reduce variability, human error, and manual labor.</li>
<li>Learn how new 21CFR part 11 enabling features in the new AssayMAP software enable walkup operation and simplify transfer of assays along the entire biotherapeutic development process, including moving from non-compliant to compliant labs.</li>
<li>Find out how documentation has been simplified and enhanced with the new automated report generation feature.</li>
<li>See the workflows that are enabled on the AssayMAP platform with new large capacity AssayMAP cartridges.</li>
</ul>
<p>Who Should Attend:</p>
<ul>
<li>Scientists doing biotherapeutic drug development from discovery to pre-clinical work.</li>
<li>People involved in quality control and assurance.  </li>
<li>People looking to increase reproducibility and throughput. </li>
<li>Scientists doing proteomics and phosphoproteomics research.</li>
</ul>
<blockquote>
<p><strong>Presenter:</strong> Steve Murphy, Ph.D. (Workflows and Applications Manager, Agilent Technologies)</p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Catherine Dold (Health &amp; Environment Writer, C&amp;EN Media Group)</p>
</blockquote>


C&EN: Automated Protein Sample Prep For Non-Automation Experts

Automated Protein Sample Prep For Non-Automation Experts

The AssayMAP Bravo is a flexible yet easy-to-use automated micro chromatography-based protein sample preparation platform.

<h5><strong>The Problem&nbsp;</strong></h5><p>When working with adenovirus (AdV) vectors it’s a big deal to get fast answers on capsid titer, empty/full ratio, and if things are aggregated. UV/Vis absorbance at 260 nm (A260) is considered the quickest check of AdV titer – but it requires denaturing your AdV, easily making it a 30 minute assay. On top of that, A260 results get thrown off by protein, DNA contamination, or just about anything else that absorbs. Other more technical methods to get titer, like qPCR, are too slow, hands-on or sample-hungry, and none are ready for a quick, easy check of your adenovirus sample.</p><h5><strong>The Solution&nbsp;</strong></h5><p>Stunner’s unique combination of UV/Vis with static and dynamic light scattering (SLS &amp; DLS) gives researchers a full read-out on AdV titer, empty/full ratio, and aggregation – in about a minute using only 2 µL.</p><h5><strong>The Proof&nbsp;</strong></h5><p>In this seminar you’ll learn how Stunner delivers dye-free, standard-free, and hassle-free titers down to 1E9 vp/mL, and checks the size and aggregation of 96 samples in just 1 hour. We’ll look at all the info Stunner delivers, how these can be used for adenoviral vector sample QC, and how adenovirus from a bunch of different vendors stacks up.<br>&nbsp;</p><blockquote><p><strong>Presenter:&nbsp;</strong>Nelis Denys (Product Manager, Unchained Labs)</p><p><strong>Moderator: </strong>Kevin Lance PhD<strong> </strong>(Marketing Manager, Analytical Instruments, Unchained Labs)</p></blockquote>

Unchained Labs: Snag spot-on adenovirus titers & empty/full ratios with Stunner

Snag spot-on adenovirus titers & empty/full ratios with Stunner

Join our webinar and check out concentration, labeling, stability, and viscosity data of a mAb and its conjugate. 

LCMS webinars focusing on Sample prep - page 24