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

Article

Webinars

Video

Scientists

Scientific article

Interview

Science and research

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

LabRulez

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

Organomation

DataApex CE - Capillary Electrophoresis Extension for Clarity

CE module provides specific terminology, evaluation by time corrected area and peak identification by peak start or end (additionally to peak apex).

<h3>Extension for Capillary Electrophoresis</h3>
The CE Extension activates the CE mode in Clarity environment and can be activated on any <a href="https://lcms.labrulez.com/products/999">Clarity</a> Instrument. CE Extension is compatible also with <a href="https://lcms.labrulez.com/products/1000">Clarity Offline</a> software. CE module provides specific terminology, evaluation by time corrected area and peak identification by peak start or end (additionally to peak apex).
<h4>Main changes in Clarity environment</h4>
<ul>
<li>CE specific terminology</li>
<li>Evaluation by time corrected area</li>
<li>Peak identification by peak start or end (additionally to peak apex).</li>
<li>Additional calculations</li>
</ul>
<h4>CE specific terminology</h4>
The terms used in chromatography mode were substituted by those used in CE:
<ul>
<li>Default mode =&gt; CE mode</li>
<li>Chromatogram =&gt; Electropherogram</li>
<li>Retention time (RT) =&gt; Migration Time (MT)</li>
<li>Column =&gt; Capillary</li>
<li>Mobile Phase =&gt; Electrolyte</li>
<li>Flow Rate =&gt; Power supply</li>
<li>Pressure =&gt; Injection Mode</li>
</ul>
<h4>Separation parameters</h4>
Method Setup allows a user to adjust the Capillary Setting:
<ul>
<li>Total Capillary Length</li>
<li>Length of the capillary.</li>
<li>Effective Capillary Length</li>
<li>Effective capillary length from injection end to the detector position</li>
<li>Separation Voltage</li>
<li>Separation voltage. Allows you to enter also negative values</li>
<li>Reference Peak Mobility</li>
<li>Effective mobility of the EOF reference peak.</li>
</ul>
<h4>Calculations</h4>
The Result Table contains additional columns containing calculations:
<ul>
<li>Apparent Mobility</li>
<li>Effective Mobility</li>
</ul>

Wiley KnowItAll Analytical Edition Software

KnowItAll by Wiley offers a comprehensive solution for identifying, analyzing, and managing analytical data, enhancing spectral analysis speed and overall lab efficiency.

Solutions for IR, MS, NMR, Raman, &amp; UV-Vis<blockquote>More information on the Wiley Science Solutions website: <a target="_blank" rel="noopener noreferrer" href="https://sciencesolutions.wiley.com/knowitall-analytical-edition-software/">KnowItAll Analytical Edition Software</a></blockquote><h5>Accelerate Spectral Analysis &amp; Boost Efficiency!</h5>KnowItAll by Wiley is an all-in-one solution for identifying, analyzing, and managing spectral data, streamlining lab workflows.<ul data-start="208" data-end="581" data-is-only-node="" data-is-last-node=""><li data-start="208" data-end="328">User-friendly interface with tools for processing, searching, mixture analysis, deconvolution, and reporting</li><li data-start="329" data-end="406">Patented spectral intelligence for automated, expert-driven workflows</li><li data-start="407" data-end="481">Supports multiple techniques &amp; vendor formats for full flexibility</li><li data-start="482" data-end="581" data-is-last-node="">Integrated with Wiley’s high-quality spectral databases for faster, more accurate results</li></ul><figure class="image"><img style="aspect-ratio:1922/1036;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Wiley_Wiley_Know_It_All_Analytical_Edition_Software_cover_a703599ad2/Wiley-Wiley-KnowItAll-Analytical-Edition-Software-cover.jpg" alt="Wiley: Wiley KnowItAll Analytical Edition Software" width="1922" height="1036"></figure><h4>Streamline Your Analysis with KnowItAll</h4>KnowItAll integrates all essential tools and data into a single, user-friendly platform, saving you time, optimizing workflows, and enhancing data interpretation.<h4>Compatible Data Types</h4>A vendor-neutral solution, KnowItAll supports 130+ instrument formats, ensuring seamless workflow continuity even as lab equipment evolves.<ul data-start="408" data-end="518"><li data-start="408" data-end="473">Spectroscopic Techniques: IR, MS, NIR, NMR, Raman, UV-Vis</li><li data-start="474" data-end="518">Chromatograms &amp; Molecular Structures</li></ul><h3 data-start="520" data-end="542">Key Features</h3>Eliminate the need for multiple software packages—KnowItAll combines powerful tools in one intuitive interface for seamless transitions between tasks.<ul data-start="701" data-end="998"><li data-start="701" data-end="750">Comprehensive Spectrum &amp; Mixture Analysis</li><li data-start="751" data-end="799">Database Management &amp; Advanced Searching</li><li data-start="800" data-end="863">Structure Drawing &amp; Professional Reporting (ChemWindow)</li><li data-start="864" data-end="907">Spectrum Processing &amp; Deconvolution</li><li data-start="908" data-end="956">Extensive Spectral Library Subscriptions</li><li data-start="957" data-end="998">Quantitative Analysis Module</li><li data-start="1030" data-end="1072">IR/Raman functional group analysis</li><li data-start="1073" data-end="1128">MS reverse &amp; adaptive search (patente)</li><li data-start="1129" data-end="1174">Automated MS deconvolution &amp; analysis</li><li data-start="1175" data-end="1212">NMR chemical shift prediction</li></ul><h4>What’s Included?</h4><h5>Data Toolbox</h5><ul data-start="1264" data-end="1540"><li data-start="1264" data-end="1318">ID Expert™ – One-click spectral identification</li><li data-start="1319" data-end="1411">SearchIt™ – Advanced database search with mixture analysis &amp; multi-technique support</li><li data-start="1412" data-end="1470">MineIt™ – Spectral database creation &amp; data mining</li><li data-start="1471" data-end="1540">QC Expert™ – Quality control for IR, Raman, and Chromatograms</li></ul><h5>Spectral Processing Toolbox</h5><ul data-start="1581" data-end="1716"><li data-start="1581" data-end="1652">MS Expert™ – GC-MS deconvolution with automated database search</li><li data-start="1653" data-end="1716">ProcessIt™ – Spectrum processing for IR, MS, NMR, Raman</li></ul><h5>Spectral Analysis Toolbox</h5><ul data-start="1755" data-end="1882"><li data-start="1755" data-end="1827">AnalyzeIt™ – Functional group analysis for IR, Raman, &amp; polymers</li><li data-start="1828" data-end="1882">PredictIt™ NMR – NMR chemical shift prediction</li></ul><h5>Basics Toolbox</h5><ul data-start="1910" data-end="2115"><li data-start="1910" data-end="1965">ChemWindow – Full-featured 2D structure drawing</li><li data-start="1966" data-end="2049">ReportIt™ – Professional reporting for structures, spectra, &amp; chromatograms</li><li data-start="2050" data-end="2115">BrowseIt™ – Web portal with KnowItAll resources &amp; updates</li><li data-start="2050" data-end="2115">Optional Quantitation Module - Enhance GC-MS, IR, Raman, UV-Vis, and GC workflows with integrated quantification.</li></ul><h5>Access High-Quality Spectral Libraries</h5><ul><li>Subscribe to Wiley’s industry-leading IR, MS, NMR, Raman, and UV-Vis spectral databases for optimal analytical accuracy.</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Wiley_Wiley_Know_It_All_Analytical_Edition_Software_Know_It_All_Spectral_Libraries_2fdbf59fd0/Wiley-Wiley-KnowItAll-Analytical-Edition-Software-KnowItAll-Spectral-Libraries.jpg" alt="Wiley: Wiley KnowItAll Analytical Edition Software - KnowItAll Spectral Libraries" width="474" height="343"><h4>System Recommendations &amp; Compatibility</h4><ul><li><a target="_blank" rel="noopener noreferrer" href="https://sciencesolutions.wiley.com/system-recommendations/">See system recommendations here.</a></li><li><a target="_blank" rel="noopener noreferrer" href="https://sciencesolutions.wiley.com/knowitall-supported-file-formats/">View file formats supported.</a></li></ul>*Subscription required to KnowItAll Spectral Libraries.

SIELC HPLC Software - HPLC.cloud

SIELC has developed the first and only HPLC software that is accessible via the cloud.

<h5>Each <a href="https://lcms.labrulez.com/products?instrumentationItems=27&amp;search=SIELC">instrument</a> is connected directly to our secure cloud server via an Ethernet line.</h5>
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/SIELC_SIELC_Software_HPLC_cloud_1_441d304d5d.jpg" alt="SIELC: SIELC Software – HPLC.cloud."/>
<h5>All instrument parameters are visible and adjustable on the fly from any internet-enabled device. Instrument settings are stored as methods, which can be retrieved and used for specific compounds.</h5>
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/SIELC_SIELC_Software_HPLC_cloud_2_f626a8f395.jpg" alt="SIELC: SIELC Software – HPLC.cloud."/>
<h5>Multiple samples can be organized in a sequence with various methods. Results can be compared and quantitated:</h5>
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/SIELC_SIELC_Software_HPLC_cloud_3_6eb75a29c9.jpg" alt="SIELC: SIELC Software – HPLC.cloud."/>
Please see an online example of the separation results <a href="https://chrom.app/share/#/samples/11972/injection/21307/?t=a992fefcdd3647b19f6bed81e182d3d8">here</a>.
<h5>With your Alltesta and HPLC.cloud free subscription, you can analyze almost any compound from the palm of your hand. For example, you can analyze the dyes that are in your favorite purple sports drink:</h5>
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/SIELC_SIELC_Software_HPLC_cloud_4_b8e9abd33a.jpg" alt="SIELC: Separation of Blue 1 and Red 40 dyes in Gatorade Zero – Grape."/>
<h5>Alternatively, you can analyze the caffeine content in your morning coffee:</h5>
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/SIELC_SIELC_Software_HPLC_cloud_5_f39557543e.jpg" alt="SIELC: Retention of Caffeine."/>
<h5>Another option is to separate and analyze the vitamin content in your daily multi-vitamin:</h5>
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/SIELC_SIELC_Software_HPLC_cloud_6_bbf8e002a3.jpg" alt="SIELC: Separation of Vitamin C and Vitamin B2."/>

Wiley KnowItAll LC-MS Database Collection

The KnowItAll LC-MS Library offers access to an impressive collection of over 2.7 million high-quality mass spectra designed to accelerate spectral identification.

<h4>KnowItAll LC-MS Library: Confident Identification Starts Here</h4>Access over 2.7 million high-quality LC-MS spectra with the KnowItAll LC-MS Library—designed to accelerate and streamline compound identification and classification.<h5>Key Features:</h5><ul><li>Includes four trusted LC-MS databases covering lipids, PFAS, polymers, drugs, and more</li><li>Each record features spectra, chemical structures, and metadata</li><li>Continuously updated to provide the latest compound coverage</li><li>Compatible with most MS instrument formats</li><li>Expert-reviewed for data accuracy and reliability</li></ul><h5>Applications:</h5>Ideal for environmental analysis, food safety, metabolomics, clinical research, QC, and more. This collection supports fast, reliable LC-MS workflows in both research and routine lab settings.<h5>Database Coverage:</h5><ul><li>LC-MS – Class Rule-Based PFAS Library: Over 7,000 spectra</li><li>LC-MS – Class Rule-Based Polymer Library: Over 202,000 spectra</li><li>LC-MS – Class Rule-Based Lipids Library: Over 2.5 million spectra</li><li>Wiley Registry of Tandem Mass Spectral Data: MSforID: 12,000 spectra</li></ul>Extend your coverage with optional NIST bundles and other spectral libraries.

Wiley KnowItAll Solutions for LC-MS

LC Expert streamlines LC-MS workflows with automated processing, deconvolution, and MS/MS or accurate mass search. Combined with KnowItAll databases, it ensures fast and complete spectral analysis.

<h4>Revolutionize Your LC-MS Workflow with KnowItAll LC Expert</h4>KnowItAll LC Expert brings speed and precision to LC-MS analysis. New in KnowItAll 2025, this tool automates deconvolution, processing, and spectral searches—turning hours of manual work into minutes.<h5>Key Features:</h5><ul><li>Automated non-targeted LC-MS/MS analysis LC Expert processes raw chromatograms, extracts components, and matches MS/MS spectra to Wiley’s trusted databases.</li><li>Targeted accurate mass identification Identify known compounds using accurate mass and structure databases with support for retention times and custom metadata.</li><li>Advanced spectral search algorithms Use patented adaptive search and MSforID algorithms to explore similar or coeluted spectra when exact matches aren’t found.</li><li>Access to premium LC-MS databases Includes millions of spectra from PFAS, polymer, lipid, and drug-related libraries. Expandable with NIST and Maurer libraries.</li><li>Database building &amp; in-house data integration Build multi-technique databases using MineIt and import existing MSP collections. Easily manage compound records and raw data.</li><li>Integrated tools for structure &amp; reporting Use ChemWindow for 2D structure drawing and ReportIt for automated documentation with spectra, tables, and annotations.</li></ul><h5>Applications Across Fields:</h5>Perfect for pharmaceuticals, forensics, metabolomics, environmental testing, cosmetics, materials science, and academic research.<h5>Compatibility:</h5>Vendor-neutral and supports multiple instruments and data formats—ensuring seamless integration and workflow continuity.Take your LC-MS analysis to the next level—faster, smarter, more reliable.Learn more at: <a target="_blank" rel="noopener noreferrer" href="https://sciencesolutions.wiley.com">sciencesolutions.wiley.com</a>

Wiley NIST/EPA/NIH Mass Spectral Library 2023

The 2023 NIST/EPA/NIH Mass Spectral Library is a major update from NIST's expert team, reflecting 40+ years of development. It’s an essential, trusted resource for accurate mass spectral analysis.

<h4>Boost Your MS Workflow with the NIST 2023 Mass Spectral Library</h4>The NIST/EPA/NIH Mass Spectral Library 2023 is a major update to one of the world’s most trusted MS databases. Developed by NIST's expert team over four decades, it remains a vital tool for GC-MS and MS/MS analysis.What's Included:<ul><li>EI Library: 394,000 spectra, 341,600 unique compounds, now with AI-RI values</li><li>MS/MS Libraries: 2.3M+ spectra, 51,500+ compounds, 399,000+ precursor ions</li><li>GC Retention Index Library: 491,700 RI values, 180,600 unique compounds</li><li>NIST Software: MS Search, AMDIS, MS Interpreter</li></ul>New in 2023:<ul><li>40,000+ new EI compounds and 43,000+ spectra added</li><li>MS/MS coverage expanded by 60% over 2020 release</li><li>Enhanced compatibility with most MS platforms via Wiley</li></ul>Even More with Wiley:<ul><li>Combine with the Wiley Registry 2023 for greater coverage</li><li>Add KnowItAll Software for advanced spectral analysis</li></ul>Compatible with most MS data systems. Learn more: <a target="_blank" rel="noopener noreferrer" href="https://sciencesolutions.wiley.com/compatibility">sciencesolutions.wiley.com/compatibility</a>

Wiley LC-MSⁿ Library of Drugs, Poisons and Their Metabolites, 2nd Edition

The Maurer/Wissenbach/Weber LC-MSⁿ Library, 2nd Ed., offers MS² and MS³ spectra for over 2,270 drugs and 3,600+ metabolites. It enables proven metabolite-based LC-MSⁿ screening and is one of the few libraries focused on metabolite spectra.

<h4>Optimize LC-MSⁿ Screening with a Proven Metabolite-Based Library</h4>The Maurer/Wissenbach/Weber LC-MSⁿ Library, 2nd Edition, offers a powerful screening method using MS² and MS³ spectra for over 2,270 parent drugs and 3,600+ metabolites. It’s one of the few libraries focused specifically on metabolite spectra, improving sensitivity, selectivity, and reducing false negatives in LC-MS analysis.Developed for clinical and forensic applications, the library helps confirm compound identity and detect metabolites even when parent analytes are suppressed. It also reduces false positives through characteristic metabolite patterns.Includes instrument-specific training materials on sample prep, chromatography, and MS settings.<h5>Library Specs:</h5><ul><li>Spectra: &gt;13,000</li><li>Structures: 10,787</li><li>Compounds: &gt;2,270</li><li>Metabolites/Artifacts: &gt;3,600</li><li>Endogenous Molecules: 90</li></ul>Search compound coverage at <a target="_blank" rel="noopener noreferrer" href="https://spectrabase.com/">compoundsearch.com</a>.

Wiley Registry of Tandem Mass Spectral Data – MSforID

The "Wiley Registry of Tandem Mass Spectral Data: MS for ID" consists of 12,048 positive and negative mode spectra of over 1,000 compounds of interest for forensics, toxicology, and pathology. 

<h4>High Mass-Accuracy LC-MS/MS Library for Confident Identification</h4>The Wiley Registry of Tandem Mass Spectral Data: MS for ID includes 12,048 spectra in positive and negative modes covering 1,163 compounds relevant to forensics, toxicology, and pathology—including drugs, pesticides, and pharmaceuticals.Developed by the Oberacher team at Innsbruck Medical University under controlled conditions, the library offers ~95% specificity and &gt;92% sensitivity. It delivers fast, reproducible results and is highly transferable across LC-MS/MS platforms.Highlights:<ul><li>12,048 spectra for 1,000+ small bioorganic molecules</li><li>Optimized for high-accuracy identification</li><li>Includes advanced LC-MS/MS search algorithm</li><li>Compatible with most instrument formats</li></ul>Search compound coverage at: <a target="_blank" rel="noopener noreferrer" href="https://www.compoundsearch.com">www.compoundsearch.com</a>

Wiley LC-HR-MS/MS Library of Drugs, Poisons and Their Metabolites

The updated MMHW LC-HR-MS/MS library offers 5,500+ spectra of drugs, poisons, and metabolites. A trusted resource for toxicology, doping control, and environmental analysis.

<h4>From the Leader in Spectral Data</h4>The Maurer, Meyer, Helfer, Weber: LC-HR-MS/MS Library of Drugs, Poisons, and Their Metabolites, 2nd Edition (MMHW) is one of the most comprehensive LC-MS resources for clinical and forensic toxicologists. Developed by Prof. Hans H. Maurer and his team, the database emphasizes metabolites essential for accurate toxicological screening.This edition contains over 5,500 high-quality spectra, covering 2,300+ parent drugs/poisons and 3,200+ metabolites or artifacts across 100+ classification groups. Substances are categorized by toxicological relevance, with accompanying methods in PDF format.The data is carefully curated and reviewed by experts, ensuring reliable compound identification. Wiley collaborates with major MS vendors, supporting multiple instruments and formats for seamless workflow integration.<h4>Applications</h4>The MMHW library is trusted worldwide for compound analysis and verification in:<ul><li>Clinical and forensic toxicology</li><li>Doping control</li><li>Environmental and food chemistry</li><li>Pharmacokinetics and pathology</li></ul><h4>What’s New</h4>The 2nd edition adds 550+ new datasets, including designer drugs, cannabinoids, opioids, stimulants, and more.<h4>Specifications</h4><ul><li>Spectra: 5,558</li><li>Structures: 4,270</li><li>Unique Compounds: 2,763</li><li>Metabolites/Artifacts: &gt;3,250</li></ul>Available in KnowItAll and NIST formats, this library remains a critical resource for accurate, sensitive, and selective LC-HR-MS/MS screening.Search compound coverage at <a target="_blank" rel="noopener noreferrer" href="https://spectrabase.com/">compoundsearch.com</a>.

DataApex Clarity Chromatography Software

Clarity is a chromatography data software for data acquisition, processing, and instrument control in regulated environment. Clarity is a flexible solution for devices from different vendors, supporting different applications.

Optional control modules provide integrated control of selected instruments such as GCs, LCs, pumps, detectors, autosamplers, etc. Extensions provide functions for specific separation techniques or calculations such as PDA, GPC analysis, Mass spectrometry, or SST. Clarity can run in English, French, German, Russian, Spanish, and Chinese language. Support technicians and developers are close to their users and ready to provide extensive Support from DataApex.
<blockquote>
Ask for <a href="https://www.dataapex.com/product/clarity-demo">Clarity Demo version</a> which allows you to get your hands on software before purchase
</blockquote>
<h3>Main features</h3>
<ul>
<li>Measuring: Simultaneous data acquisition from up to four independent chromatographs, each chromatograph can acquire data from up to 32 detectors.
</li>
<li>Integration: There is an extensive possibility to modify chromatograms. The chromatogram can be changed by entering global parameters or interactively through direct graphic modification of the baseline.
</li>
<li>Overlay: Simultaneously displays a virtually unlimited number of chromatograms and their mathematical modification; for example, mutual deductions or derivations of any order.
</li>
<li>Calibration: Internal and external standard calculation methods, calibration of groups of peaks, and reference peaks method for better identification.
</li>
<li>Wide range of supported instruments: Control modules in Clarity allow users to control various instruments in their lab. See our growing <a href="https://www.dataapex.com/controls">List of supported instruments</a>.
</li>
<li>Extensions completing your workflow: Clarity Extensions integrates your workflow into one application. GPC calculations, PDA data processing, gas or detailed hydrocarbon analyses according to selected norms, and much more.
</li>
<li>Automated measuring support: Sequence tables for any set of samples with or without an autosampler.
</li>
<li>Postrun: Automatically displays, prints, exports, and starts other programs after the completion of a measurement.
</li>
<li>Summary result tables: Displays and prints selected results from all simultaneously displayed chromatograms.
</li>
<li>User settings: User selects parameters for peak display and the specification for axes, including color from an extensive array of color settings. Text labels and lines, either as part of the area or anchored to a chromatogram, may also be inserted.
</li>
<li>Export: Optional exportation of all results, with or without the chromatogram, in various formats, into a file or clipboard.
</li>
<li>Import: Imports chromatograms or mathematical curves, which have been saved in text or AIA formats, from other programs.
</li>
<li>LIMS: Clarity offers connectivity with LIMS, both for sample submission and result output. This can be done via convenient ASCII transfers.
</li>
<li>Method and calibration history: Each chromatogram can easily be displayed under the same conditions as when it was printed, exported, or saved.
</li>
<li>Column performance: Calculations of peaks in terms of symmetry, efficiency, resolution; all by several methods (tangent, moments, etc.).
</li>
<li>Batch: Automatically batch processes, displays, exports, or prints any number of chromatograms.
</li>
<li>User calculations: Users can define custom calculations in the Result and Summary tables. Using the integrated editor, you can create your own columns from original columns and individual mathematical functions.
</li>
<li>User accounts: Sets up access rights and passwords (including their parameters, e.g., minimum length, validity, etc.). Each user can define his or her own appearance of the software.
</li>
<li>Audit trail: Records selected events and operations into a special file. Records selected operations directly into a chromatogram.
</li>
<li>Electronic signature: Each chromatogram can be signed electronically. Signature selection is based on the username or the signature certificate.
</li>
<li>Networked Solution: Clarity chromatography software files can be accessed from networked computers using Clarity Offline software. This enables the offline evaluation of chromatograms, development of new methods, and printing reports. See the <a href="https://gcms.labrulez.com/products/1000">Clarity Offline</a> for more details.
</li>
<li>Language Localizations available: Useful for non-English speakers. At the moment, there are French, German, Russian, Spanish, and Chinese localizations available in a single installation package. Simply switch to your preferred language anytime.
</li>
<li>Competitive approach: The chromatography market offers many specialized HPLC data systems or GC data systems; these are often provided with the purchased instrument. It is usually complicated to integrate such software into the workflow of the laboratory since they do not enable direct control of additional instruments. Compared to other small-scale solutions, Clarity offers a wide range of directly controlled instruments as well as optional Extensions for specific separation techniques. On the other hand, complex solutions with a wide scope of features and scalable design are quite expensive, which is a limiting factor for many customers. Another drawback of the large solutions is their complexity which imposes high demands on users. Compared to this, Clarity represents a scalable medium-ranged solution with a steep learning curve and competitive prices.
</li>
</ul>
<h3>Clarity configurations examples</h3>
<h4>One chromatograph with two detectors</h4>
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Data_Apex_Clarity_Chromatograficky_Software_Clarity_configurations_examples_One_chromatograph_with_two_detectors_ae482b83b8/DataApex-Clarity-Chromatograficky-Software-Clarity-configurations-examples-One-chromatograph-with-two-detectors.jpg" alt="DataApex Clarity Chromatography Software: Clarity configurations examples - One chromatograph with two detectors.jpg"/>
<ul>
<li>The HPLC measures on two detectors. Clarity will acquire two separate signals sharing a common timebase (synchronized START/STOP). A resulting chromatogram will contain two signals.</li>
</ul>
<h4>Two chromatographs, one with multiple detectors</h4>
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Data_Apex_Clarity_Chromatograficky_Software_Clarity_configurations_examples_Two_chromatographs_one_with_multiple_detectors_b21dc07faf/DataApex-Clarity-Chromatograficky-Software-Clarity-configurations-examples-Two-chromatographs-one-with-multiple-detectors.jpg" alt="DataApex Clarity Chromatography Software: Clarity configurations examples - Two chromatographs, one with multiple detectors.jpg"/>
<ul>
<li>This example displays a configuration with two chromatography systems (GC + HPLC) where the HPLC system uses multiple detectors. All the detectors attached to the HPLC Instrument will share common timebase (synchronized START/STOP). The GC detector will be independent.</li>
</ul>
<h4>Two chromatographs, one digital control</h4>
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Data_Apex_Clarity_Chromatograficky_Software_Clarity_configurations_examples_Two_chromatographs_one_digital_control_1bf9cec334/DataApex-Clarity-Chromatograficky-Software-Clarity-configurations-examples-Two-chromatographs-one-digital-control.jpg" alt="DataApex Clarity Chromatography Software: Clarity configurations examples - Two chromatographs, one digital control.jpg"/> This example displays a configuration with two chromatography systems (GC + LC). The GC is connected and controlled via digital interface *, using a GC Control appropriate module.
<h4>Four chromatographs with autosampler each</h4>
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Data_Apex_Clarity_Chromatograficky_Software_Clarity_configurations_examples_Four_chromatographs_with_autosampler_each_945873d808/DataApex-Clarity-Chromatograficky-Software-Clarity-configurations-examples-Four-chromatographs-with-autosampler-each.jpg" alt="DataApex Clarity Chromatography Software: Clarity configurations examples - Four chromatographs with autosampler each.jpg"/>
<ul>
<li>This example displays a configuration with two chromatography systems (GC + LC). The GC is connected and controlled via digital interface *, using a GC Control appropriate module.</li>
</ul>
<a href="https://www.dataapex.com/controls">List of supported instruments</a>
<a href="https://www.dataapex.com/product/clarity-std-compatibility">Compatible Windows OS and Hardware</a>
<a href="https://www.dataapex.com/product/clarity-21cfr-compliance">Clarity 21 CFR Part 11 compliance</a>

Products focused on Software distributed by LabRulez - page 1

Related content

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

Webinars LabRulezLCMS Week 07/2026

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