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

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

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

Webinars LabRulezLCMS Week 07/2026

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

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

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<p><strong>UV-VIS-NIR can be a powerful analysis technique in battery research and development. Whether it is studying new materials, monitoring electrolytes for degradation, or conducting measurements in situ using fiber optics, UV-VIS-NIR measurement capability can support applications from production to end-of-life recycling.</strong></p><p>Agilent's portfolio of instruments offers the high performance and flexible accessories needed for pioneering new applications.</p><blockquote><p><strong>Presenter:</strong> Scott Melis, PhD (Application Scientist, Agilent Technologies, Inc.)</p><p>Scott Melis has a PHD in Physics from Georgetown University in Washington, DC and started with Agilent in 2021 as a Molecular Spectroscopy Application Scientist. In his graduate work, Scott studied nanoparticle formation and growth for a variety of applications. Projects that he worked with include developing processes to deposit and characterize semiconducting molecular nano-cocrystals for use in optoelectronic devices as well as controlling polymer nanoparticle size through rapid mixing conditions.</p></blockquote>

Agilent Technologies: UV-VIS-NIR in Battery Development

UV-VIS-NIR in Battery Development

Agilent's portfolio of instruments offers the high performance and flexible accessories needed for pioneering new applications.

<header><p><strong>Join Us for an Engaging Live Webinar on Integrating UV/Vis Spectroscopy Into Your Laboratory Workflows</strong></p></header><main><div><div><p><strong>Program&nbsp;</strong></p><ul><li>Introduction to UV/Vis Spectroscopy</li><li>The Power of Integration</li><li>Live Demonstration</li><li>Customer Use Cases</li><li>Engage &amp; Discuss</li></ul></div></div><div><div><p>Discover how connecting your UV/Vis spectrophotometer with instruments like balances can transform your laboratory processes. By transmitting dissolution data directly to the spectrophotometer, you can streamline workflows and enhance data quality, leading to improved productivity and accuracy.</p></div></div><div><div><div><p>In this informative session, we’ll showcase the power of instrument integration and how it can revolutionize your daily routines. Using real-world case studies from various industries, including battery manufacturing, pharmaceuticals, and food and beverage, you’ll gain valuable insights into optimizing your laboratory workflows.</p><p><strong>Program Highlights</strong></p><ul><li><strong>Introduction to UV/Vis Spectroscopy</strong><br>Understand the basics and applications of UV/Vis spectroscopy in laboratories.</li><li><strong>The Power of Integration</strong><br>Explore the benefits of connecting your UV/Vis spectrophotometer with balances and other instruments.</li><li><strong>Live Demonstration</strong><br>Witness a live demonstration of data transmission from a balance to a UV/Vis spectrophotometer.</li><li><strong>Customer Use Cases</strong><br>Learn about integrated processes used in the battery, pharma, and food &amp; beverage industries.</li><li><strong>Engage &amp; Discuss</strong><br>Participate in a Q&amp;A session where we address your questions and discuss potential applications in your own lab.</li></ul><p>Don’t miss this opportunity to explore innovative solutions that can help you think critically about your own processes and enhance your laboratory's efficiency!</p></div></div></div></main><div><div><p><strong>Target Audience</strong></p><div><p>This webinar is designed for laboratory professionals, scientists, and managers across various industries, including:</p><ul><li>Pharmaceuticals: Quality control and research &amp; development teams looking to improve analytical processes</li><li>Food &amp; Beverage: Quality assurance and product development personnel aiming to enhance product testing efficiency</li><li>Battery Manufacturing: Engineers and technicians interested in optimizing material testing workflows</li><li>Laboratory Managers: Professionals seeking to streamline operations and improve data quality through instrument integration</li></ul><p>Whether you are just starting with UV/Vis spectroscopy or looking to enhance your existing laboratory workflows, this webinar is perfect for you. Register now to secure your spot and take the first step towards a more efficient laboratory.</p><ul><li><span style="padding-right:0px;" id="webinar-session-1"><strong>1. 10. 2025 9:00,&nbsp; English&nbsp;</strong></span><span id="webinar-session-2"><strong><svg width="16" height="16" viewBox="0 0 16 16" fill="none" xmlns="http://www.w3.org/2000/svg"></svg></strong></span></li><li><span id="webinar-session-2"><strong>1. 10. 2025 17:00,&nbsp; English&nbsp;</strong></span></li></ul><blockquote><p><span id="webinar-session-2"><strong>Presenter: </strong></span>Anika Adams (Product Manager, SPG UV/VIS)</p><div><p>Anika Adams is Product Manager for UV/Vis Spectrophotometers at METTLER TOLEDO, where she focuses on driving innovation and optimizing customer workflows. With a degree in business administration and experience spanning software development, mechanical engineering, and production, Anika brings a multidisciplinary perspective to the laboratory business. Her expertise lies in automating and enhancing customer processes, ensuring both product excellence and customer satisfaction.</p><p><strong>Presenter:</strong> Dr. Fabian Müller (Product Manager, SPG UV/VIS)</p><div><div><div><div><p>Dr. Fabian Müller, Ph.D., is an accomplished chemist from the ETH Zürich in Switzerland. After completing his doctoral studies, Dr. Müller joined the team at METTLER TOLEDO as an Application Specialist for UV/Vis spectroscopy, where he quickly established himself as a skilled and knowledgeable professional. His expertise in this area led to his promotion to the position of Product Manager for UV/Vis spectrophotometers.</p></div></div></div></div></div></blockquote></div></div></div>

Mettler Toledo: UV/Vis Integration in Laboratory Workflows 

UV/Vis Integration in Laboratory Workflows 

Join Us for an Engaging Live Webinar on Integrating UV/Vis Spectroscopy Into Your Laboratory Workflows

<div><p><strong>Join us for the last 5 series on building the perfect method for light scattering analysis.</strong></p><p><strong>Learn advanced tools and techniques to master ASTRA software, from normalization to DLS with flowing systems.</strong></p><h4><strong>Session Overview:</strong></h4><ul><li><h5><strong>Part 6 of 10: Building the Perfect Method - Normalization, Alignment, &amp; Inter-Detector Band Broadening Corrections</strong></h5><ul><li>Friday, September 26</li></ul></li><li><strong>Part 7 of 10: </strong>Navigating Sample Parameters – A Close Look at dn/dc and Extinction Coefficients<ul><li>Friday, October 3</li></ul></li><li><strong>Part 8 of 10: </strong>Advanced Characterization Tools for Multi-Component Analytes - Protein Conjugates, AAV, LNP and ADC<ul><li>Friday, October 10</li></ul></li><li><strong>Part 9 of 10: </strong>ASTRA for Particles: When and How to Deploy<ul><li>Friday, October 17</li></ul></li><li><strong>Part 10 of 10: </strong>DLS with Flowing Systems – Leveraging Rh and the Burchard-Stockmayer Plot in ASTRA<ul><li>Friday, October 24</li></ul></li></ul><h4><strong>Why Attend:</strong></h4><ul><li>Deepen your understanding of light scattering and ASTRA.</li><li>Gain actionable insights for your lab.</li><li>Interact with our expert, Dr. Andy Meyer.</li></ul><p>The live interactive web series are 100% live sessions, with anonymous Q&amp;A welcome during and after the discussion. Free for all Wyatt customers.</p><blockquote><p><strong>Hosted by:</strong> Dr. Andy Meyer</p><p>Dr. Andy Meyer joined Wyatt Technology in 2001, serving for several years as an Applications Scientist, then as Dean of Wyatt's "Light Scattering University" and as Director of Customer Service &amp; Support. After managing multiple regions in North America, Dr. Meyer is now a Principal Trainer for Waters | Wyatt Technology. As a Wyatt customer, he completed his Ph.D. in Applied Science – Polymer Chemistry from the College of William and Mary in Virginia.</p></blockquote></div>

Waters Corporation: Becoming an ASTRA Expert

Becoming an ASTRA Expert: Part 6

Learn essential method setup steps in ASTRA: normalization, alignment, and band broadening corrections for optimal accuracy in light scattering experiments.

<div><p><strong>Analytical methods are essential to ensuring pharmaceutical product quality, regulatory compliance, and patient safety. However, their reliability and reproducibility can be compromised by multiple sources of variability—including reagent quality, instrument performance, operator technique, sample preparation, and data processing. Understanding and controlling these sources is critical, especially when justifying post-approval changes to validated methods.</strong></p><p>This three-part webinar series features expert Peter Baker (Live Oak QA, Austin, Texas) and focuses on the importance of identifying, monitoring, and documenting variability within analytical workflows. Through open discussion and real-world insights, participants will gain a deeper understanding of how to build a scientifically sound case for method adjustments while maintaining regulatory compliance. Each session includes a live Q&amp;A to encourage interaction and address specific challenges.</p><h4><strong>Session 3: Analytical Control in Action – Real-World Case Studies</strong></h4><p>The final session presents real-world examples of method variability and how companies have successfully justified changes due to shifts in materials, instruments, or processes. Emphasis will be placed on documentation, regulatory communication, and lessons learned.</p><p><i><strong>Goal: </strong>Apply insights from case studies to your own workflows and gain practical strategies for managing change.</i><br>&nbsp;</p><blockquote><p><strong>Presenter:</strong> Peter Baker (President, Live Oak Quality Assurance LLC)</p><p>Peter E. Baker, President, Live Oak Quality Assurance LLC, has been consulting nationally and internationally since April 2019. Prior to consulting, Peter spent 11 years as a U.S. FDA Drug Investigator, with most of those years spent working in FDA’s overseas offices located in India, China and Chile. Peter was named FDA Investigator of the Year in 2013 for his work uncovering serious breaches in data integrity and has special interest in data governance and compliance with 21 CFR Part 11. Live Oak focuses on training and employee empowerment in critical thinking, with the goal of improving the quality of medicines through good data management.</p><p><strong>Presenter: </strong>Dr. Stephanie Harden (Senior Manager, Small Molecule Core Solutions – LC-MS, Waters Corporation)</p><p>Stephanie Harden, Senior Manager at Waters Corporation, leads the Product Marketing and Scientific teams for Waters small molecule HPLC portfolio. With over 25 years of experience in product and segment marketing, she has a proven track record in strategic program development, cross-functional leadership, and market-driven innovation. Her work connects scientific insight with commercial strategy to drive customer-focused solutions and sustained business growth. Stephanie holds a PhD in Chemistry from the University of Bristol, UK, and is a widely cited author.</p></blockquote></div>

Waters Corporation: Managing Method Variability: A Foundation for Risk-Based Change

Managing Method Variability: A Foundation for Risk-Based Change - Session 3

Discover real case studies on managing analytical variability, documenting changes, and maintaining compliance in pharma workflows.

Analytical Control in Action – Real-World Case Studies

<div><div container-id="cq-colctrl-lt0" comp-id="A1"><div><p><strong>Biopharmaceuticals based on monoclonal antibodies, lipid nanoparticle-encapsulated mRNA, and transgene-carrying viral vectors, are significantly larger than traditional small-molecule drugs. This size difference requires specialized analytical tools. Size-exclusion chromatography (SEC) is particularly effective for studying proteins and has recently been adapted to analyze complex macromolecular assemblies like mRNA and DNA.</strong></p><p>Join us for this exciting two-part webinar series where Dr. Jelle De Vos from RIC group and Dr. Sonja Schneider from Agilent Technologies will discuss how SEC is evolving to meet the demands of modern biopharma. In Part 2, our experts will share real-world application examples of SEC with light scattering detection, highlighting how this powerful combination is transforming the analysis of complex biopharmaceuticals.</p><h5><strong>Key learning objectives of Part 2:</strong></h5><ul><li>Understand the practical application of SEC for the characterization of:<ul><li>monoclonal antibodies</li><li>mRNA-lipid nanoparticle formulations</li><li>adeno-associated viruses (AAVs)</li><li>virus-like particles (VLPs)</li></ul></li></ul><h5><strong>Who should attend?</strong></h5><ul><li>Scientists and researchers in biotherapeutics R&amp;D using SEC/light scattering.</li><li>Lab and quality leaders, including lab managers, directors, and QA/QC professionals in biopharma production.</li></ul><h5><strong>Want to go back and watch Part 1?</strong></h5><p><strong>Click here to register for Part 1</strong>, and hear the fundamentals of SEC and discover how coupling it with light scattering detection can advance the characterization and development of biopharmaceuticals.</p><h5><strong>Certificate of attendance</strong></h5><ul><li>If you attend the live webinar, you will automatically receive a certificate of attendance, including a learning outcomes summary, for continuing education purposes.</li><li>If you view the on-demand webinar, you can request a certificate of attendance by emailing editor@selectscience.net.</li></ul><blockquote><p><strong>Presenter: </strong>Dr. Jelle De Vos (Senior Scientist, RIC group)</p><p>Dr. Jelle De Vos currently works at the RIC group as an expert in developing chromatography methodologies for analyzing complex biopharmaceutical samples. His work focuses on pushing the boundaries of modern separation science, and he has published over 40 articles on advancing the limits of ultra high-performance liquid chromatography and developing microfluidic technology.</p><p><strong>Presenter:&nbsp;</strong>Dr. Sonja Schneider (Scientist, Application Development, Agilent Technologies)</p><p>Dr. Sonja Schneider is an Application Scientist at Agilent Technologies in Waldbronn, Germany, who has published numerous application notes on the analysis of biopharmaceuticals. After obtaining her PhD in proteomics in 2011, she started as an Application Scientist for Bioanalytics and has been working various kinds of critical quality attributes of monoclonal antibodies, mRNA, and LNPs.&nbsp;</p><p><strong>Moderator:</strong> Olivia Long (Editorial Team, SelectScience)</p></blockquote></div></div></div>

SelectScience: Part 2: Size exclusion chromatography with light scattering for biopharmaceuticals

Part 2: Size exclusion chromatography with light scattering for biopharmaceuticals

Explore real-world SEC with light scattering for antibodies, mRNA-LNPs, AAVs, and VLPs. Insights from Agilent and RIC group experts.

SEC with light scattering for biopharmaceuticals

<p><strong>Dr. Michaela Nebel, Product Manager at Sensolytics GmbH, gives an overview of the theory of localized electrochemical techniques with a focus on Scanning Electrochemical Microscopy (SECM), Scanning Droplet Cell technique (SDC), and Scanning Electrochemical Cell Microscopy (SECCM). Then, application examples from different fields in electrochemistry, including electrocatalysis, corrosion research, and sensors are highlighted.</strong></p><p>In recent years, the rising inclusion of localized electrochemical analysis into classical electrochemical methods has allowed for more comprehensive characterization of sample surfaces from various fields of application.</p><h5><strong>Key learnings of this webinar:</strong></h5><ul><li><strong>Theoretical background of localized electrochemical techniques</strong> with a focus on Scanning Electrochemical Microscopy (SECM), Scanning Droplet Cell technique (SDC), and Scanning Electrochemical Cell Microscopy (SECCM)</li><li><strong>Guidelines for the selection</strong> of a localized technique fitting your individual research application</li><li><strong>Practical considerations</strong> for the use of the respective analysis method</li><li><strong>Selected applications</strong> from different fields of research, including electrocatalysis, corrosion research, and sensors</li></ul><blockquote><p><strong>Presenter: </strong>Dr. Michaela Nebel (Product Manager at Sensolytics GmbH)</p></blockquote>

Metrohm: Introduction to Localized Electrochemical Techniques

Introduction to Localized Electrochemical Techniques

Learn SECM, SDC, and SECCM fundamentals and applications in electrocatalysis, corrosion research, and sensors. Practical guidance from experts.

<div><div container-id="cq-colctrl-lt0" comp-id="A1"><div><p><strong>As global food safety regulations become increasingly stringent and consumer scrutiny intensifies, laboratories are under pressure to deliver rapid, accurate results while managing complex sample matrices.</strong></p><p>Analyzing emerging contaminants such as PFAS, pesticides, veterinary drugs and other residues in processed or high-fat foods poses significant challenges in method robustness, instrument uptime and data reliability.</p><p>This webinar will explore how the QSight 500 LC-MS/MS is addressing these evolving demands to provide high-quality data for even the most demanding food matrices.</p><h5><strong>Attend this webinar to:</strong></h5><ul><li>Gain insights into how to optimize your LC-MS/MS workflows for better efficiency and confidence in your results</li><li>Understand how to reliably detect contaminants across complex matrices&nbsp;</li><li>Learn how the QSight 500 LC-MS/MS system brings greater operational efficiency with reduced instrument cleaning&nbsp;</li><li>Explore how enhancing system robustness reduces cost per sample&nbsp;</li></ul><blockquote><p><strong>Presenter: </strong>Jamie Foss (Product Manager, Liquid Chromatography &amp; Mass Spectrometry at PerkinElmer)</p><p>Jamie Foss is the Liquid Chromatography and Mass Spectrometry Product Manager at PerkinElmer. Prior to this role, he was a Sr. Application Scientist developing strategic applications in support PerkinElmer’s LC and LC/MS product portfolio. He has developed a wide variety of applications across food, environmental, industrial, forensics and cannabis. Prior to joining PerkinElmer in 2016, he spent 4 years as a forensic chemist for the State of Maine where he focused on the analysis of controlled substances and clandestine laboratory investigation.</p></blockquote></div></div></div>

Technology Networks: Addressing Evolving Demands in Food Analysis

Addressing Evolving Demands in Food Analysis

Optimize food contaminant analysis with QSight 500 LC-MS/MS. Robust, efficient workflows for PFAS, pesticides, and residues in demanding food matrices.

<div><div container-id="cq-colctrl-lt0" comp-id="A1"><div><p><strong>Prof. Thalassinos's research focuses on understanding how cells respond to DNA damage using single-cell proteomics. The study employs a compound called 60G to induce DNA damage, which activates DNA repair mechanisms such as mismatch repair, base excision repair, and nucleotide excision repair. By analyzing single cells, the research aims to uncover the variability in protein expression and the biological processes involved in DNA repair and apoptosis.</strong></p><p>The team uses advanced techniques like the Orbitrap Eclipse mass spectrometer and the SLN1 single-cell isolation system to isolate and analyze individual cells. This approach allows them to observe the upregulation of proteins involved in DNA repair and the arrest of cells in the S phase of the cell cycle. The findings highlight the importance of single-cell proteomics in revealing cellular heterogeneity and the dynamic response to DNA damage, which could have implications for understanding diseases like cancer and neurodegenerative disorders.&nbsp;</p><h5><strong>Learning points:</strong></h5><ul><li><strong>Single-Cell Proteomics Advantage: </strong>Single-cell proteomics allows for the observation of individual cellular responses to DNA damage, revealing heterogeneity that would be masked in bulk proteomics. This approach helps in understanding the specific activation of DNA repair mechanisms and cell cycle arrest at the S phase.&nbsp;</li><li><strong>DNA Repair Mechanisms: </strong>The study highlights the activation of various DNA repair pathways, such as mismatch repair, base excision repair, and nucleotide excision repair, in response to DNA damage induced by the compound 60G. This understanding is crucial for insights into diseases like cancer and neurodegenerative disorders.&nbsp;</li><li><strong>Technological Integration: </strong>The use of advanced technologies like the <strong>Orbitrap Eclipse</strong> mass spectrometer and the SLN1 single-cell isolation system enables precise isolation and analysis of single cells, facilitating detailed proteomic studies and enhancing the understanding of cellular processes at a granular level.&nbsp;</li></ul><h5><strong>Who should attend:</strong></h5><ul><li><strong>Cancer Researchers: </strong>Understanding the variability in DNA repair mechanisms at the single-cell level can provide insights into tumor heterogeneity and the development of targeted cancer therapies.</li><li><strong>Neurodegenerative Disease Scientists</strong>: Insights into DNA damage response mechanisms can aid in understanding the molecular basis of neurodegenerative diseases and potentially lead to new therapeutic strategies.&nbsp;</li><li><strong>Proteomics and Genomics Technologists:</strong> Professionals working with advanced proteomics and genomics technologies can benefit from the presentation's focus on cutting-edge techniques for single-cell analysis, enhancing their research capabilities and methodologies.&nbsp;</li></ul><p>If you cannot attend this webinar please register to receive a link to the On Demand version the following day.&nbsp;</p><blockquote><p><strong>Presenter: </strong>Prof. Konstantinos Thalassinos (Professor, University College London)</p><p>Kostas moved to the UK in 1998 to study for a BSc in Genetics at the University of Leicester, having completed his high school education in his native Greece. After graduation he went on to the University of York to undertake a Masters in Bioinformatics, which included a three-month industrial placement writing software to process mass spectrometric data. Having gained an interest in mass spectrometry, Kostas then went to the University of Warwick in order to pursue a PhD that combined experimental and computational studies in mass spectrometry-based proteomics. After being awarded his PhD in 2006, Kostas was the successful recipient of a one-year Wellcome Trust Value in People Fellowship. Post-doctoral training followed and in 2010 he moved to the Institute of Structural and Molecular Biology at University College London / Birkbeck to take up a lectureship in biophysical mass spectrometry and has been there ever since. In 2015 he was promoted to Senior Lecturer and in 2019 to Professor of mass spectrometry.</p><p>His lab is using structural mass spectrometry approaches, especially ion mobility and crosslinking, to study the structure and dynamics of proteins and protein complexes, particularly those involved in protein misfolding diseases.</p></blockquote></div></div></div>

Thermo Fisher Scientific: ASMS 2025 Workshops

Probing DNA-damage response at the single cell level

Explore single-cell proteomics in DNA damage research. See how Orbitrap Eclipse and SLN1 reveal repair mechanisms, cell cycle arrest, and disease insights.

<p><strong>New functions of the improved UV Workstation Software will be described and demonstrated.</strong></p><blockquote><p><strong>Presenter:&nbsp;</strong> Scott Melis, PhD (Application Scientist, Agilent Technologies, Inc.)</p><p>Scott Melis has a PHD in Physics from Georgetown University in Washington, DC and started with Agilent in 2021 as a Molecular Spectroscopy Application Scientist. In his graduate work, Scott studied nanoparticle formation and growth for a variety of applications. Projects that he worked with include developing processes to deposit and characterize semiconducting molecular nano-cocrystals for use in optoelectronic devices as well as controlling polymer nanoparticle size through rapid mixing conditions.</p></blockquote>

Agilent Technologies: New Software Features for UV Work Station Software

New Software Features for UV Work Station Software

New functions of the improved UV Workstation Software will be described and demonstrated.

<h4><strong>Our newest HPLC columns are game changing</strong></h4><h5><strong>Liquid chromatography is evolving</strong></h5><p>With growing demands for sensitivity, reproducibility, and speed, today’s workflows need column technology that can keep up. Whether you are analyzing trace-level compounds or navigating complex bioseparations, the right column makes all the difference.</p><p>A new generation of LC column technology is setting the bar higher—delivering cleaner separations, sharper peaks, faster equilibration, and more reliable results for even the most metal-sensitive analytes.</p><h5><strong>Want to see it in action?</strong></h5><p>Join our webinar to explore how this new column technology transforms oligonucleotide separations for characterization, sequencing, and impurity profiling.</p><blockquote><p><strong>Presenter:&nbsp;</strong> Dr. Anne Blackwell (Product Manager Bio LC Columns, Agilent Technologies)</p><p>Anne is a product manger for bio LC columns at Agilent, with previous experience as a product support scientist for bio LC columns and an LC/MS applications scientist focused on metabolomics. &nbsp;She has a Ph.D. in analytical chemistry from the University of Arizona where she studied mass spectrometry of non-covalent protein assemblies.</p><p><strong>Presenter: </strong>Dr. Andrew Coffey (Senior Application Scientist, Agilent Technologies)</p><p>Andrew Coffey joined Agilent Technologies Biocolumns Applications Team in 2011. &nbsp;He has over 35 years experience in method development, technical support and troubleshooting of reversed phase, ion exchange, size exclusion and many other liquid chromatographic techniques.</p></blockquote>

Agilent Technologies: Inert Separations for Oligo LC-MS Workflows

Inert Separations for Oligo LC-MS Workflows

Explore Agilent’s new HPLC columns in a webinar on advanced oligonucleotide separations, sequencing, and impurity profiling.