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

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

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

Webinars LabRulezLCMS Week 07/2026

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

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

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

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.

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Shimadzu Corporation

While the application of Mass Spectrometry (MS) Imaging is rapidly growing, its usage is largely limited to experienced scientists. Shimadzu’s Benchtop MALDI-TOF, however, offers a compact, affordable, and user-friendly option to all. Moreover, when combined with the automated matrix applicator (iMLayer suite), our Benchtop MALDI-TOF provides a game-changing solution suitable to all users regardless of skill level.
In this webinar, we will showcase how our workflow offers simplified sample preparation, a complete imaging solution in a compact footprint, an imaging starter kit customizable based on your needs, and intuitive software for data analysis. This workflow will be suitable in research applications from analysis of small molecules such as lipids to large molecules such as protein, peptides, polymers etc.
Join us to learn how you can become an expert in MS imaging with Shimadzu&#39;s MALDI-TOF today.
Learning Objectives:
<ul>
<li>Learn how Shimadzu offers total solutions for MALDI Imaging</li>
<li>Learn about our patented Two-step Vapour Deposition Method for optimal sample preparation</li>
<li>Learn about our user-friendly interface for easy data analysis of MALDI Images</li>
<li>Applications of Shimadzu&#39;s Benchtop MALDI Imaging suite</li>
</ul>
<blockquote>
Presenter: Naatasha Isahak (Product Specialist, Shimadzu (Asia Pacific) Pte Ltd)
</blockquote>
<blockquote>
Naatasha Isahak is a Product Specialist for MALDI and Life Sciences Products from Shimadzu Asia Pacific Pte Ltd. She has received her PhD from the University of Sydney (Chemistry) working on surface initiated polymerisation on silica nanoparticles using RAFT polymerisation and bioorthogonal conjugation of peptides using Native Chemical Ligation. She then spent 5 years working on developing platforms for stem cells and organoids characterization that included working with microfluidic devices and helical polymers. Naatasha joined Shimadzu in 2022 to expand her experiences to MALDI characterization on materials and biological samples.
</blockquote>

Shimadzu: MALDI-Imaging For All: A Researcher’s Guide

MALDI-Imaging For All: A Researcher’s Guide

Join us to learn how you can become an expert in MS imaging with Shimadzu's MALDI-TOF today.

Dear user and other PaSER interested customers,
You are hereby invited to our 2nd Virtual PaSER Workshop. A lot of new possibilities has been introduced since last time – including, but not limited to PaSER Novor for de novo sequencing of dda-PASEF® data on the PaSER Box as well as TIMS DIA-NN 2.0 -which will be demonstrated during this Workshop. Data virtualization has been a requested feature – and this is now possible with Mass Dynamics for PaSER. Not limited to above – stay tuned for even more approaching features, we will discuss as well.
<h3>The tentative agenda looks like this:</h3>
<h5>1:00 – 1:15 pm: Introduction</h5>
<ul>
<li>Willy Bjørklund</li>
</ul>
<h5>1:15 – 1: 35pm: New Applications on the timsTOF Platform</h5>
<ul>
<li>Lars Kristensen (Field Application Specialist)</li>
</ul>
<h5>1:35 – 1:55 pm: PaSER as a bioinformatic platform - what’s new and what’s coming</h5>
<ul>
<li>Jonathan Krieger (Software R&amp;D Department)</li>
</ul>
<h5>5 minute break</h5>
<h5>2:00 – 2:20 pm: Live Demo/workshop of PaSER</h5>
<ul>
<li>Tharan Srikumar (Software R&amp;D Department)</li>
</ul>
<h5>2:20 – 2:50 pm: Mass Dynamics</h5>
<ul>
<li>Mark Condina and Giuseppe Infusini</li>
</ul>
<h5>2:50 – 3:10 pm: Questions and discussions</h5>
<h5>3:10 – 3:15 pm: Conclusion</h5>
<ul>
<li>Willy Bjørklund</li>
</ul>
We aim for a lively interaction so take the timing as an indication. Please feel free to share with colleagues or others you think could benefit from attending this workshop. Looking forward to “meet”

Bruker Virtual PaSER Workshop

Dear user and other PaSER interested customers, You are hereby invited to our 2nd Virtual PaSER Workshop. 

This webinar will focus on untargeted LC/MS Omics solutions that will provide the biological insights needed to produce meaningful results. An emphasis will be spent on an End-to-End HILIC metabolomics workflow for our LC/Q-TOF platform.
This includes automate sample preparation for cells and plasma, a Bio LC that is fit for purpose for metal sensitive analysis, robust and transferable HILIC chromatography, the 6546 LC/Q-TOF data independent analysis of samples, with an ID workflow that includes a new HILIC PCDL with 500 core metabolism analytes with spectra and retention time annotation.
For unknowns not found in Agilent PCDLs, SIRIUS/CSI:FingerID which uses AI predict structure from spectra and conducts online identification search will be demonstrated. A complementary targeted multi-omics workflow will be briefly mentioned before sharing the new Ion Mobility and ExD technologies for high end LC/MS Omics investigations.
<blockquote>
Presenter: Karen E. Yannell (Omics Workflow Specialist, Agilent Technologies)
</blockquote>
<blockquote>
Karen E. Yannell is an Omics Workflow Specialist at Agilent Technologies. She is an expert in small molecule high throughput analysis by triple quadrupole (TQ) and quadrupole time-of-flight (Q-TOF) mass spectrometry for applied markets. Her recent work has focused on developing targeted metabolomics methods and routine Q-TOF workflows for both expert and non-expert users alike. Previously, Karen worked on forensic, metabolomics, and biomarker discovery applications with ambient ionization sources. She received her PhD in Analytical Chemistry from Purdue University where studied under the advisement of Prof. R. Graham Cooks. 
</blockquote>
<blockquote>
Presenter: Dr. Martin Graf-Utzmann (Editor, Wiley Analytical Science, Moderator)
</blockquote>
<blockquote>
Dr. Martin Graf-Utzmann has a Ph.D. in Theoretical Chemistry and is an editor for Wiley Analytical Science. His interests are mainly Laboratory Automation, Digitalization, and Lab Equipment.
</blockquote>

Wiley Analytical Science: Jump Start Your LC/Q-TOF Omics Investigation with Reliable Workflows

Jump Start Your LC/Q-TOF Omics Investigation with Reliable Workflows

This webinar will focus on untargeted LC/MS Omics solutions that will provide the biological insights needed to produce meaningful results.

Your LC/Q-TOF Omics Investigation with Reliable Workflows

Thousands of polymeric compounds and materials have been developed over the years to optimize the properties and performance of products spanning nearly every industry. There are a few areas where characterizing these products can be important: first is performing a quick polymer identification for recycling purposes; second is quality control to identify product defects or failures; and third is reverse engineering to facilitate product development in a highly competitive marketplace.
Infrared (IR) and Raman spectroscopy are especially useful for the analysis of polymers in an industrial setting because in most cases it does not require sample preparation or expensive consumables. Examples will be presented demonstrating the effectiveness of IR and Raman analysis in each of these categories.
Mass Spectrometry (MS) has become an indispensable tool for polymer analysis and has been widely used to study polymer structure and composition, end groups and additives, molecular weight distribution, and so on. MS analysis is extremely sensitive, allowing the detection and identification of minor polymer components and synthesis by-products, as well as low-level impurities and products of decomposition. Matrix Assisted Laser Desorption Ionization (MALDI) allows performing rapid MS analysis without lengthy pre-separation and with minimal sample preparation. MALDI MS can provide structural and copolymer composition information, as well as be used for imaging of polymer surfaces, characterization of complex polymer mixtures, and many other analytical tasks.
In this webinar, we will discuss several MS analytical techniques and their applications for polymer analysis using real-life examples from the industry and academia.
<blockquote>
Presenter: Sergey V. Shilov, Ph.D. (R&amp;D Product Manager for North America, Bruker Optics)
</blockquote>
<blockquote>
Dr. Sergey V. Shilov is the R&amp;D Product Manager for North America at Bruker Optics. Sergey joined Bruker in 2001. He is responsible for the support and development of new applications for the Bruker research FTIR systems. He received his Ph.D in 1992 from the Russian Academy of Sciences in Polymer Physics and his M.S. from St. Petersburg State University (Russia) in Physics in 1986. Alexander Von Humboldt foundation (Germany) awarded him research fellowship in 1996. Sergey published 37 papers in peer-reviewed journals. His research interests include time-resolved FTIR spectroscopy, surface science, polymer and life-science applications. 
</blockquote>
<blockquote>
Presenter: Kushal Modi (Business Development Manager, Polymers, and Industrial Chemicals, Bruker Applied Mass Spectrometry)
</blockquote>
<blockquote>
Kushal Modi has been serving the scientific community for over 10 years. He joined Bruker in 2022 under the Applied Mass Spectrometry division after a legacy with Waters Corporation. He is a leading expert as a Business Development Manager and is currently supporting the polymers and industrial chemical markets nationally. 
</blockquote>
<blockquote>
Presenter: Dr. Rebecca Pool (Editor Microscopy and Analysis, Wiley, Moderator)
</blockquote>
<blockquote>
Rebecca is news editor of Microscopy&amp;Analysis and a freelance science journalist with a doctorate in Materials Science. She has published in Wiley Analytical Science, Nature Photonics, SPIE Photonics Focus, Physics World, Sci Fi Generation, Engineering and Technology magazine, WorldSteel and more.
</blockquote>

Wiley Analytical Science: Effective Analysis of Polymers Using IR, Raman Spectroscopy, and MALDI-TOF Mass Spectrometry

Effective Analysis of Polymers Using IR, Raman Spectroscopy, and MALDI-TOF Mass Spectrometry

Examples will be presented demonstrating the effectiveness of IR and Raman analysis and will discuss several MS techniques and apps for polymer analysis.

Polymers Using IR, Raman Spectroscopy, and MALDI-TOF MS

A novel spatial technique, DISCO-MS, combines whole-organ/whole-organism clearing and imaging, deep-learning-based image analysis, robotic tissue extraction, and ultra-high-sensitivity mass spectrometry with the Bruker timsTOF instrument family. This combination enables DISCO-MS to perform unbiased proteome analysis of preclinical and clinical tissues from quantity-limited materials after unbiased imaging of entire specimens in 3D.
In this webinar, you will learn about a new experimental approach that combines whole tissue clearing, dia-PASEF®, and trapped ion mobility spectrometry (TIMS) mass spectrometry to analyze the spatial proteome of complex tissue structures. The webinar will detail how with this technique, researchers were able to:
<ul>
<li>Analyze the proteome of preclinical and clinical tissues after identification of regions of interest using 3D imaging, followed by robotic tissue extraction</li>
<li>Achieve early unbiased detection and characterization of subtle tissue perturbations across pathologies</li>
<li>Benefit from the use of ultra-high sensitivity and robust timsTOF mass spectrometers</li>
</ul>
<h5>Key learning objectives</h5>
<ul>
<li>Discover the new experimental approach that combines whole tissue clearing, dia-PASEF®, and TIMS mass spectrometers can be used to analyze the spatial proteome of complex tissue structures</li>
<li>Understand how researchers were able to analyze the proteome of specific tissue regions following 3D imaging to enable robotic tissue extraction</li>
<li>Learn about the unparalleled sensitivity and robustness the timsTOF platform offers with 4D-Proteomics™ which enables researchers to delve deeper into proteome analysis and gain greater insights</li>
</ul>
<blockquote>
Presenter: Dr. Harsharan Singh Bhatia (Institute for Tissue Engineering and Regenerative Medicine (iTERM))
</blockquote>
<blockquote>
Dr. Harsharan Singh Bhatia is the Omics technologies team leader at the Institute for Tissue Engineering and Regenerative Medicine (iTERM), Helmholtz Munich. He completed his Ph.D. at the University of Freiburg, Germany, studying the neuroprotective role of dietary antioxidants. Bhatia worked as a postdoctoral researcher at UCLA, where he investigated the impact of dietary manipulations on rodent behavior. He later returned to the University of Freiburg to work as a research associate at the University Clinic, exploring epigenetic factors&#39; regulation of microglial function. In 2017, Bhatia joined iTERM to study chronic neuroinflammation using DISCO tissue clearing and spatial-omics tools.
</blockquote>
<blockquote>
Presenter: Jemima Arnold (Editorial Team, SelectScience)
</blockquote>
<blockquote>
Jemima studied Cellular and Molecular Medicine at the University of Bristol, UK, and as a member of the Editorial team, she now plays an integral role in shaping the content on SelectScience.
</blockquote>

SelectScience: Spatial proteomics in three-dimensional intact specimens

Spatial proteomics in three-dimensional intact specimens

A new experimental approach that combines whole tissue clearing, dia-PASEF®, and TIMS MS to analyze the spatial proteome of complex tissue structures.

<ul>
<li>Wait what?! Who knew!? There are so many things that a mass spec can do.
</li>
<li>I&#39;ve used it for years, yes this may be true.
</li>
<li>I&#39;ve processed some samples, more than a few.
</li>
<li>But between me and you, I had no idea all the things it could do!
</li>
<li>From sample prep to separation, you just won&#39;t believe…
</li>
<li>All of the tips and tricks we have up our sleeve.
</li>
<li>So, take a few minutes, about 15 should do.
</li>
<li>And learn all the things your mass spec can do.
</li>
</ul>
An easy to follow guide detailing how to set MS scan parameters for an LCMS experiment will be presented. Scan speeds for reproducible quantitation, chromatographic resolution, retention time definition, proper threshold adjustment for optimum datafile size, and how this can result in faster processing times will all be discussed.
<blockquote>
Presenter: Rebecca Glaskin, Ph.D. (LC/MS Application Scientist, Agilent Technologies, Inc.)
</blockquote>
<blockquote>
Rebecca Glaskin is an LC/MS Application Scientist at Agilent with a focus on BioPharma applications supporting the LC-Q/TOF and IM-QTOF platforms. Prior to joining Agilent, Rebecca received her Ph.D. in analytical chemistry from Indiana University in the lab of Professor David Clemmer. While there she designed and constructed home-built instruments, pushing the limits of the mobility resolution that can be obtained with a circular drift tube for the separation of biomolecules (peptides, proteins, carbohydrates, and metabolites). While there, she also studied hydrogen/deuterium exchange of proteins in the gas-phase as a function of time and pressure. Rebecca then went to Boston University as a Postdoctoral Associate in the lab of Professor Catherine Costello to develop a database containing collision cross section values for glycans, peptides, and glycopeptides utilizing Agilent Technologies 6560 IM-QTOF. This database can be used to determine how the collision cross section is altered with the addition of individual saccharide units. The trendlines obtained from this database will be used to predict collision cross sections for glycopeptides based on the conformation and structure of the specific glycoform.
</blockquote>
<blockquote>
Presenter: Jim Lau, PhD (HRAMS LC/MS Application Engineer, Agilent Technologies, Inc.)
</blockquote>
<blockquote>
Jim Lau received his Ph.D. From the University of Colorado. There he worked in the laboratories of Peter Albersheim and Robert Shapiro. This work involved the structure elucidation of plant natural products and, in particular, elucidating the structures of oligosaccharides derived from plant cell wall polysaccharides. This work was done in the early days of LCMS and made use of DLI-LCMS and (at the time) recently invented Thermospray-LCMS.
</blockquote>
<blockquote>
After the completion of his Ph.D., Jim joined Hewlett-Packard to work on LCMS ionization techniques with Paul Goodley during the early days of Electrospray-LCMS. He then moved to work on field applications and collaborations with Hewlett-Packard’s LCMS customers. More than 30 years later, Jim continues to work with Agilent’s customers in High Resolution Accurate Mass applications of LCMS. While involved in many areas of HRAMS LCMS, his recent work has focused on the area of Screening/Qual&amp;Quant of small molecules and on the high throughput confirmation of oligonucleotide synthesis.
</blockquote>

Agilent Technologies: How to set MS Scan Parameters for your LCMS Experiment

How to set MS Scan Parameters for your LCMS Experiment

An easy to follow guide detailing how to set MS scan parameters for an LCMS experiment will be presented.

<ul>
<li>Wait what?! Who knew!? There are so many things that a mass spec can do.
</li>
<li>I&#39;ve used it for years, yes this may be true.
</li>
<li>I&#39;ve processed some samples, more than a few.
</li>
<li>But between me and you, I had no idea all the things it could do!
</li>
<li>From sample prep to separation, you just won&#39;t believe…
</li>
<li>All of the tips and tricks we have up our sleeve.
</li>
<li>So, take a few minutes, about 15 should do.
</li>
<li>And learn all the things your mass spec can do.
</li>
</ul>
The acquisition parameters for an LCMSMS experiment can seem overwhelming. This presentation will examine the scan parameters available for designing an MSMS, explain their intended function, and suggest approaches to use based on the goal of the LCMSMS experiment. Parameters for MSMS trigger thresholds, active exclusion settings for different types of experiments and variable weighting of precursors will be discussed.
<blockquote>
Presenter: Rebecca Glaskin, Ph.D. (LC/MS Application Scientist, Agilent Technologies, Inc.)
</blockquote>
<blockquote>
Rebecca Glaskin is an LC/MS Application Scientist at Agilent with a focus on BioPharma applications supporting the LC-Q/TOF and IM-QTOF platforms. Prior to joining Agilent, Rebecca received her Ph.D. in analytical chemistry from Indiana University in the lab of Professor David Clemmer. While there she designed and constructed home-built instruments, pushing the limits of the mobility resolution that can be obtained with a circular drift tube for the separation of biomolecules (peptides, proteins, carbohydrates, and metabolites). While there, she also studied hydrogen/deuterium exchange of proteins in the gas-phase as a function of time and pressure. Rebecca then went to Boston University as a Postdoctoral Associate in the lab of Professor Catherine Costello to develop a database containing collision cross section values for glycans, peptides, and glycopeptides utilizing Agilent Technologies 6560 IM-QTOF. This database can be used to determine how the collision cross section is altered with the addition of individual saccharide units. The trendlines obtained from this database will be used to predict collision cross sections for glycopeptides based on the conformation and structure of the specific glycoform.
</blockquote>
<blockquote>
Presenter: Jim Lau, PhD (HRAMS LC/MS Application Engineer, Agilent Technologies, Inc.)
</blockquote>
<blockquote>
Jim Lau received his Ph.D. From the University of Colorado. There he worked in the laboratories of Peter Albersheim and Robert Shapiro. This work involved the structure elucidation of plant natural products and, in particular, elucidating the structures of oligosaccharides derived from plant cell wall polysaccharides. This work was done in the early days of LCMS and made use of DLI-LCMS and (at the time) recently invented Thermospray-LCMS.
</blockquote>
<blockquote>
After the completion of his Ph.D., Jim joined Hewlett-Packard to work on LCMS ionization techniques with Paul Goodley during the early days of Electrospray-LCMS. He then moved to work on field applications and collaborations with Hewlett-Packard’s LCMS customers. More than 30 years later, Jim continues to work with Agilent’s customers in High Resolution Accurate Mass applications of LCMS. While involved in many areas of HRAMS LCMS, his recent work has focused on the area of Screening/Qual&amp;Quant of small molecules and on the high throughput confirmation of oligonucleotide synthesis.
</blockquote>

Agilent Technologies: How to design an LCMSMS Experiment

How to design an LCMSMS Experiment

The scan parameters available for designing an MSMS, explain their intended function, and suggest approaches to use based on the goal of the LCMSMS experiment.

Webinar in collaboration with the Polish Society of Metabolomics.
<h3>14:00 - 14:20 Benefits of Trapped Ion Mobility Spectrometry (TIMS) for Metabolomics and Lipidomics</h3>
<ul>
<li>Presenter: Dr. Stefanie Wernisch ( Business Development Manager Metabolomics/Multiomics, Bruker Daltonics Bremen, Germany)</li>
</ul>
After revolutionizing the area of proteomics, trapped ion mobility spectrometry (TIMS) is now conquering the fields of metabolomics and lipidomics. Bruker&#39;s unique timsTOF technology addresses the complexity of biological samples by adding an orthogonal dimension of separation before mass spectrometric analysis, thus reducing the complexity of MS/MS data and improving annotation confidence for untargeted analysis. The ability to determine Collisional Cross Sections (CCS) can further aid identification and outlier detection in lipidomics studies.
<h3>14:20 - 14:40 SpatialOMx® for in-depth 4D-Lipidomics™</h3>
<ul>
<li>Presenter: Dr. Janina Oetjen (Application Specialist MALDI Imaging, Bruker Daltonics Bremen, Germany)</li>
</ul>
The combined possibilities of ESI and MALDI in one instrument enables powerful SpatialOMx® applications. In short, ion mobility-based annotation can connect confident LC-TIMS-MS/MS identification with meaningful spatial information from MALDI Imaging, specifically in the field of lipidomics. Further, segmentation results based on lipid imaging can define specific regions of interest for subsequent, in-depth analysis. Thus, the information content of MALDI Imaging can be enhanced with SpatialOMx® workflows on the timsTOF fleX platform.
<h3>14:40 - 15:00 Application Round-up: 4D-Metabolomics™ and 4D-Lipidomics™</h3>
<ul>
<li>Presenter: Dr. Matthias Szesny (Application Scientist Metabolomics, Bruker Daltonics Bremen, Germany)</li>
</ul>
We will highlight the capabilities of the timsTOF platform and introduce new applications, method developments, and software solutions in the field of metabolomics and lipidomics. Those help scientists gain a faster and deeper understanding of diverse research areas such as health and disease as well as agriculture.

Bruker: Expanding the Horizons of 4D-Metabolomics and 4D-Lipidomics

Expanding the Horizons of 4D-Metabolomics and 4D-Lipidomics

Benefits of TIMS for Metabolomics and Lipidomics. SpatialOMx for in-depth 4D-Lipidomics, Application Round-up: 4D-Metabolomics and 4D-Lipidomics.

Studies on drug metabolism aid in evaluating the pharmacokinetics, pharmacodynamics and safety during discovery and development. In vitro studies of drug metabolism are essential for identifying major metabolism pathways. These studies often use accurate mass spectrometry to ensure comprehensive profiling and identification of drug metabolites. However, confident identification of drug metabolites remains challenging due to insufficient fragment ion coverage.
Here, an alternative fragmentation technique is applied to produce additional fragment ions and an informative MS/MS spectra for metabolite identification. An end-to-end workflow is demonstrated for streamlined method development and metabolite identification from high-quality and more informative electron activated dissociation (EAD) MS/MS spectra. 
Attend this webinar to learn how to:
<ul>
<li>Perform confident drug metabolite identification using alternative fragmentation mechanism</li>
<li>Harness the informative and rich data collection from the latest generation QTOF technology for sensitive drug metabolite identification</li>
<li>Employ an end-to-end workflow for drug metabolite identification, from method development to data analysis</li>
</ul>
<blockquote>
Presenter: Rahul Baghla (Global Pharma Applications Lead, SCIEX)
</blockquote>

Technology Networks: Improving End-to-End Metabolite Identification by LC-MS/MS

Improving End-to-End Metabolite Identification by LC-MS/MS

Here, an alternative fragmentation technique is applied to produce additional fragment ions and an informative MS/MS spectra for metabolite identification. 

Normative pathways for immune tolerance can be hijacked in disease, such as in metastatic cancer progression and in tuberculosis (TB). To understand the network of cells and tissues behind immune tolerance, spatial transcriptomics combined with MALDI mass spectrometry can be employed to map the distribution of transcripts, lipids and glycans. These insights can be used to discover regulatory pathways that can be targeted for diagnostic and therapeutic purposes.
In this webinar, Dr. Angelo will showcase his research into understanding the evolving spatiotemporal network behind how immune tolerance develops in cancer, pregnancy and TB.
Attend this webinar to: 
<ul>
<li>Learn about mass spectrometry-based spatial biology techniques</li>
<li>Understand tissue structure-function relationships in disease</li>
<li>Hear about how normative pathways for immune tolerance are hijacked in disease</li>
</ul>
<blockquote>
Presenter: Dr. Michael Angelo (Assistant Professor Stanford University)
</blockquote>

Bruker: Spatially Encoded Pathways for Immune Tolerance in Human Health and Disease

Spatially Encoded Pathways for Immune Tolerance in Human Health and Disease

Dr. Angelo will showcase his research into understanding the evolving spatiotemporal network behind how immune tolerance develops in cancer, pregnancy and TB.

LCMS webinars focusing on LC/TOF - page 25