<p><strong>🎤Alex Brody</strong></p><p><strong>In this episode of Concentrating on Chromatography, we sit down with Alex Brody, an organic chemist at Aqua America, to discuss the rigorous analytical methods required for regulated drinking water testing.</strong></p><p>Alex walks us through the multi-step PFAS detection process using EPA Method 537.1, including extraction, nitrogen blowdown concentration, and LC-MS analysis. He explains why sample preparation and quality control are critical for achieving trace-level detection—and why these methods can't be rushed or simplified, even with new technologies available.</p><p>We also explore taste and odor investigations, disinfection byproducts, and volatile organic compounds, plus the surprising reality of why regulated labs move slowly when adopting new instrumentation. You'll learn about the quality control checkpoints, peer review processes, and the misconceptions surrounding analytical turnaround times in compliance labs.</p><h5><strong>Topics Covered:</strong></h5><ul><li>Role of organic chemistry in regulated drinking water labs</li><li>EPA compliance requirements and regulatory bodies (EPA, PA-DEP)</li><li>PFAS detection using Method 537.1 and LC-MS</li><li>The critical importance of nitrogen blowdown sample concentration</li><li>Taste and odor analysis: MIB, Geosmin, and unknown compound identification</li><li>Why regulated methods evolve slowly (validation timelines, approval processes)</li><li>Quality control procedures: calibration checks, matrix spikes, surrogate standards, internal standards</li><li>Automated sample preparation and lab efficiency</li><li>Future PFAS regulations and Method 533 expansion</li></ul><h5><strong>Ideal For:</strong></h5><ul><li>Analytical chemists and environmental lab professionals</li><li>Water utilities and compliance officers</li><li>Chromatography practitioners interested in regulated workflows</li><li>Anyone curious about how drinking water safety is ensured</li></ul><h2><strong>Video Transcription</strong></h2><h3><strong>Ensuring Safe Drinking Water Through Advanced Analytical Chemistry</strong></h3><h4><strong>Insights from a Regulated Water Testing Laboratory</strong></h4><p>Analytical laboratories responsible for regulated drinking water testing operate under strict compliance frameworks to ensure the delivery of safe and reliable water supplies. In this interview, Alex, an organic chemist at Aqua America, outlines the scope of analytical work conducted in a modern water quality laboratory. The team primarily focuses on the determination of taste- and odor-causing compounds, disinfection byproducts, volatile organic compounds (VOCs), and per- and polyfluoroalkyl substances (PFAS). These analyses rely heavily on <strong>GC-MS and LC-MS instrumentation</strong>, supported by rigorous maintenance programs to ensure continuous operational performance and data reliability.</p><h4><strong>Regulatory Compliance and Quality Control in Drinking Water Analysis</strong></h4><p>Operating as a regulated drinking water laboratory requires adherence to stringent requirements established by agencies such as the <strong>U.S. Environmental Protection Agency (EPA)</strong> and state-level regulatory bodies. Compliance is driven by extensive quality control protocols integrated into every analytical batch. Typical workflows include calibration verification, matrix spike recovery assessments, internal standard monitoring, and surrogate performance checks. Notably, analytical batches are often limited in sample number to accommodate a substantial proportion of quality control samples, reflecting the critical importance of data defensibility in regulatory reporting.</p><p>One common misconception is the perceived speed at which results can be delivered. In reality, comprehensive sample preparation, including extraction procedures and validation steps, can extend turnaround times to a full working day or longer. Additionally, validated regulatory workflows impose limitations on the rapid adoption of new analytical technologies, as method modifications must undergo formal evaluation and approval before implementation.</p><h4><strong>Analytical Strategies for Taste and Odor Investigations</strong></h4><p>Taste and odor events represent a significant operational challenge for water utilities. Standard targeted methods are routinely applied for compounds such as <strong>2-methylisoborneol (MIB)</strong> and <strong>geosmin</strong>, which are commonly associated with earthy or musty sensory characteristics. When targeted analysis does not reveal the source, laboratories employ <strong>broad-scan GC-MS screening</strong> combined with spectral library interpretation to identify potential causative compounds. In some cases, sensory evaluation panels complement instrumental analysis, providing preliminary insight into potential treatment-related or environmental influences affecting water quality.</p><h4><strong>PFAS Monitoring: Methodological Complexity and Trace-Level Sensitivity</strong></h4><p>PFAS determination represents a rapidly evolving priority in drinking water monitoring. The laboratory currently applies <strong>EPA Method 537.1</strong>, with efforts underway to expand capabilities through certification for <strong>Method 533</strong>, thereby broadening analyte coverage. Analytical workflows typically involve solid-phase extraction followed by solvent evaporation using nitrogen-assisted blow-down techniques to achieve the trace-level sensitivity required for regulatory compliance. This concentration step is essential because PFAS compounds remain non-volatile under controlled evaporation conditions, enabling enhanced detection performance upon reconstitution and LC-MS analysis.</p><h4><strong>Future Directions in Drinking Water Analytics</strong></h4><p>Looking ahead, the primary technological driver in regulated water analysis is the demand for <strong>increasingly lower detection limits</strong> and expanded compound coverage. While regulatory frameworks can slow methodological innovation, laboratories continue to pursue efficiency improvements, such as automated sample preparation systems and optimized analytical workflows. These advances support the growing need to process high sample volumes while maintaining the stringent data quality standards required for public health protection.</p><p>Ultimately, the work performed in regulated drinking water laboratories represents a critical intersection of analytical chemistry, environmental monitoring, and public safety. Continuous methodological refinement, coupled with advances in mass spectrometry and sample preparation technologies, will play a central role in addressing emerging contaminants and ensuring long-term water quality assurance.</p><blockquote><p><strong>This text has been automatically transcribed from a video presentation using AI technology. It may contain inaccuracies and is not guaranteed to be 100% correct.</strong></p></blockquote><blockquote><h4><strong>Concentrating on Chromatography Podcast</strong></h4><p>Dive into the frontiers of chromatography, mass spectrometry, and sample preparation with host David Oliva. Each episode features candid conversations with leading researchers, industry innovators, and passionate scientists who are shaping the future of analytical chemistry. From decoding PFAS detection challenges to exploring the latest in AI-assisted liquid chromatography, this show uncovers practical workflows, sustainability breakthroughs, and the real-world impact of separation science. Whether you’re a chromatographer, lab professional, or researcher you'll discover inspiring content!</p><p>You can find <strong>Concentrating on Chromatography Podcast </strong>in podcast apps:</p><ul><li><a target="_blank" rel="noopener noreferrer" href="https://open.spotify.com/show/1wZg67rCjoGju4yhqxI3tL"><strong>Spotify</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podcasts.apple.com/tz/podcast/concentrating-on-chromatography/id1788429185"><strong>Apple podcast</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podscan.fm/podcasts/concentrating-on-chromatography"><strong>podscan</strong></a></li></ul><p>and on <a target="_blank" rel="noopener noreferrer" href="https://www.youtube.com/@ChromatographyTalk/videos"><strong>YouTube channel</strong></a></p></blockquote>

Regulated Drinking Water Testing: PFAS Detection, Sample Prep & Real Lab Insights

<p><strong>This study investigates how ionization polarity influences the gas-phase stability of native-like proteins analyzed by ion mobility spectrometry–mass spectrometry. While proteins generally retain folded structures in both positive and negative electrospray ionization modes, significant differences in unfolding behavior were observed.</strong></p><p>Proteins exhibited greater gas-phase stability when analyzed in the ionization polarity corresponding to their solution-phase charge, requiring higher energy for unfolding. These findings emphasize the importance of considering protein isoelectric points and ionization polarity in native IMS-MS experiments to ensure accurate structural characterization.</p><blockquote><h4><strong>The original article</strong></h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c04295"><strong>Investigating the Effect of Isoelectric Points on the Gas-Phase Stability of Native-like Proteins Analyzed in Positive- versus Negative-Ion Mode by IMS-MS</strong></a></h4><p>Alexis N. Edwards, Madeline G. Bannon, Michael S. Cordes, and Elyssia S. Gallagher*</p><p>Anal. Chem. 2026, 98, 6, 4518–4527</p><p><a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.analchem.5c04295">https://doi.org/10.1021/acs.analchem.5c04295</a></p><h6>licensed under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/"><strong>CC-BY 4.0</strong></a></h6></blockquote><p><strong>Selected sections from the article follow. Formats and hyperlinks were adapted from the original.</strong></p><div><p>In native mass spectrometry (nMS), the native-like structures of proteins are maintained in the gas phase by preserving the secondary, tertiary, and quaternary structures. <a href="javascript:void(0);">(1−7)</a> The preservation of native-like protein structures is primarily accomplished via the use of electrospray ionization (ESI), a soft ionization method that forms a distribution of multiply charged protein ions. These multiply charged ions can then be investigated to characterize stoichiometry, oligomeric composition, and ligand binding. <a href="javascript:void(0);">(8−10)</a></p><p>During ESI, a potential is applied to the sample-containing solution. In an aqueous spray solvent, H<sub>3</sub>O<sup>+</sup> and OH<sup>–</sup> are produced in positive-ion mode (+ESI) and negative-ion mode (−ESI), respectively. <a href="javascript:void(0);">(11)</a> The buildup of like-charges within the solution results in the formation of a Taylor Cone at the capillary tip, which ejects charged droplets that travel toward the inlet of the mass spectrometer. Droplets undergo evaporation and fission until complete analyte desolvation, leading to the release of folded, gas-phase protein ions. As the droplets shrink, H<sub>3</sub>O<sup>+</sup> or OH<sup>–</sup> can become concentrated, causing the pH of the droplet to decrease or increase, respectively. Shifts in pH can denature proteins. Therefore, to maintain native-like protein structures, nMS is conducted with solutions containing volatile salts, usually ammonium acetate, that provide ionic strength and minimize pH changes compared to spraying from pure water. <a href="javascript:void(0);">(11,12)</a> Droplet pH in ESI is influenced by flow rate, solvent composition, and applied voltage, <a href="javascript:void(0);">(13)</a> but often approaches values near the p<i>K</i><sub>a</sub> of acetate (4.76) or ammonium (9.25) in +ESI or −ESI, <a href="javascript:void(0);">(12,14)</a> respectively. During ESI, changes in overall protein charge take place via proton transfer at chargeable amino acid residues, resulting in the formation of protonated or deprotonated protein ions with the charged sites being dependent on the relative proton affinities of ammonium, acetate, and chargeable amino acids as proteins near complete desolvation. <a href="javascript:void(0);">(15−19)</a></p><p>Ion mobility spectrometry (IMS) measures an ion’s mobility through an inert gas under the influence of an electric field. Thus, mobility is directly influenced by the ion’s size, shape, and charge. <a href="javascript:void(0);">(20)</a> A protein’s mobility can be used to estimate its structure by calculating an average momentum-transfer collisional cross section (CCS). In addition to structural characterization, IMS-MS can investigate the gas-phase stability of protein complexes when paired with collision-induced unfolding (CIU). Specifically, in CIU experiments, protein ions are accelerated into a cell filled with inert gas molecules and undergo multiple collisions with higher frequency and energy relative to IMS. This converts kinetic energy to internal, vibrational energy, disrupting noncovalent interactions and inducing unfolding of the protein ions. <a href="javascript:void(0);">(21)</a> Unfolding alters the protein structure, which can then be quantified by monitoring the protein’s mobility during subsequent IMS-MS measurement. <a href="javascript:void(0);">(22)</a> Prior work with mutant proteins has shown that proteins with similar intramolecular interactions have similar CIU fingerprints, while proteins with different intramolecular interactions have different CIU fingerprints. <a href="javascript:void(0);">(23)</a> Therefore, gas-phase protein stability is correlated with intramolecular interactions.</p><p>Past native IMS-MS work has primarily been conducted in +ESI given that -ESI has the reputation of being unreliable for native-like protein analysis due to the occurrence of corona discharge, <a href="javascript:void(0);">(24)</a> and charge-state distributions that may not be representative of folded proteins. <a href="javascript:void(0);">(25)</a> In recent years, −ESI has been increasingly used in CIU and IMS-MS, with recent work demonstrating that −ESI-MS is capable of discerning denatured and native-like protein structures. <a href="javascript:void(0);">(26,27)</a> Prior work showed that charge manipulation of folded proteins, such as charge reduction, to achieve similar absolute charge states in both ion modes, results in CCS values of protein cations that are comparable to their anion counterparts. <a href="javascript:void(0);">(26,28)</a> This suggests that gas-phase structures are weakly dependent on protein charge and ionization polarity. <a href="javascript:void(0);">(23,26,28)</a> Yet, Hong et al. showed that, in the absence of charge reduction, the gas-phase stability of two proteins (avidin and β-lactoglobulin) is sensitive to ionization polarity, highlighting that gas-phase stability is not consistent between +ESI and −ESI. <a href="javascript:void(0);">(29)</a></p><h4><strong>Materials and Methods</strong></h4><h5><strong>Native IMS-MS Analysis</strong></h5><p>Glass capillaries were pulled using a P-1000 micropipette puller (Sutter Instrument Company, Novato, CA). Samples and calibrants were sprayed from pulled capillaries (inner diameter ∼1 μm) and analyzed with a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/152"><strong>Synapt G2-S High-Definition MS </strong></a>(Waters Corporation, Milford, MA). The trap and transfer cells contained Ar, the helium cell contained He, and the IMS cell contained N<sub>2</sub>. IMS wave velocity was 350 m/s, while IMS wave height was either 7 or 9 V, depending on the protein size (see <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c04295/suppl_file/ac5c04295_si_001.pdf">Table S2</a>). Proteins with larger mass required a wave height of 9 V to ensure that all the ions migrated out of the IMS cell prior to the next ion injection. Mass spectra were collected and signal averaged over 30 s. Additional instrument details can be found in the Supporting Information (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c04295/suppl_file/ac5c04295_si_001.pdf">Table S2</a>).</p><p>To limit systematic error due to repositioning of the ESI tip between runs, <a href="javascript:void(0);">(48)</a> the <i>XYZ</i>-stage position was optimized and kept consistent for all replicates. Approximately 5 μL of sample was loaded into a glass capillary, which was then mounted on the <i>XYZ</i>-stage. Electric potential was delivered to the sample by a platinum wire inserted into the capillary and placed in contact with the solution. The voltage applied to the tip holder ranged from 0.60 to 1.2 kV for native samples, and 0.80 to 1.40 kV for denatured samples. Nine replicates in each ion mode were collected for all proteins with measurements spread across 8 days over 3 weeks. These replicates were conducted in pairs by collecting data in both ion modes consecutively. To accomplish this, a CIU experiment was collected in +ESI before the instrument polarity was changed to −ESI. A second CIU experiment was performed, beginning with −ESI to counteract any changes in protein stability due to pH changes during ESI. <a href="javascript:void(0);">(14)</a> This allowed for use of the same capillary, at the same position in relation to the instrument inlet, for each +ESI/–ESI replicate pair. A new tip was used for each +ESI/–ESI replicate pair. CIU experiments were accomplished by increasing collision voltage (CV) to the trap cell in 5 V steps, from 0 V to a maximum of 120 V.</p><h4><strong>Results and Discussion</strong></h4><p>Ten proteins were chosen for analysis in +ESI and −ESI in this work (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c04295#tbl1">Table 1</a>). These proteins can be broken into three groups depending on the net-charge in solution at pH 7: net-negative (with pI &lt; 6.5), net-neutral (with 6.5 ≤ pI ≤ 7.5), and net-positive (with pI &gt; 7.5). Five of the ten proteins have a net-negative charge at pH 7, though four of these proteins (con A, β-lactoglobulin, ovalbumin, and α-lactalbumin) are routinely analyzed via +ESI-IMS-MS. <a href="javascript:void(0);">(18,28)</a> Additionally, each protein had charge-state distributions in +ESI and −ESI that resulted in at least one overlapping charge state (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c04295#fig1">Figure 1</a>), allowing for direct comparison of <sup>TW</sup>CCS<sub>N2→He</sub> and CIU50 in both ion modes.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Anal_Chem_2026_98_6_4518_4527_Figure_1_Representative_mass_spectra_in_ESI_top_and_ESI_bottom_cb81976247.jpg" alt="Anal. Chem. 2026, 98, 6, 4518–4527: Figure 1. Representative mass spectra in +ESI (top) and −ESI (bottom) for (A) ovalbumin, (B) GNA, (C) β-lactoglobulin, (D) α-lactalbumin, (E) con A, (F) streptavidin, (G) ubiquitin, (H) WGA, (I) cytochrome c, and (J) lysozyme. Proteins that have blue or red charge states indicate additional oligomeric states that were detected. Outlines in red boxes are overlapping charge states that are compared herein. *Indicates contaminant peaks." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Anal_Chem_2026_98_6_4518_4527_Figure_1_Representative_mass_spectra_in_ESI_top_and_ESI_bottom_cb81976247.jpg 245w," sizes="100vw" width="1600" height="865"></p><h5><strong>Proteins with Disulfide Bridges are Stable in Both Polarities</strong></h5><p>For both lysozyme and α-lactalbumin, the average <sup>TW</sup>CCS<sub>N2→He</sub> were within experimental uncertainty in +ESI and −ESI for both the initial, folded structures and the final, extended structures (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c04295#tbl2">Table 2</a>). However, the 6+ and 6- ions of lysozyme and α-lactalbumin showed a high resistance to unfolding with &gt;90% of the ions retaining their folded <sup>TW</sup>CCS<sub>N2→He</sub> values even at high CV (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c04295#fig2">Figure 2</a>). Replicate data showed similar trends (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c04295/suppl_file/ac5c04295_si_001.pdf">Figure S2</a>). While CCS values provide a description of gas-phase structures, CIU experiments provide information on the stability of the gas-phase protein structures. Furthermore, the number and pattern of disulfide bridges present in antibodies has been characterized by CIU. <a href="javascript:void(0);">(63)</a> Lysozyme and α-lactalbumin both contain the glycosyl hydrolases family 22 (GH22) domain, which has four disulfide bridges that span ∼94% and ∼93% of the amino acid sequence, respectively (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c04295/suppl_file/ac5c04295_si_001.pdf">Figure S3</a>). Thus, we hypothesize that rather than effects from protein pI and ionization polarity, the unfolding behavior of these proteins is controlled to a greater extent by the presence of stabilizing disulfide bridges that prevent routine unfolding during collisional activation.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Anal_Chem_2026_98_6_4518_4527_Figure_2_Representative_mobiligrams_showing_arrival_times_for_lysozyme_A_C_and_a_lactalbumin_B_D_0f3d23c3c1.jpg" alt="Anal. Chem. 2026, 98, 6, 4518–4527 - Figure 2. Representative mobiligrams showing arrival times for lysozyme (A, C) and α-lactalbumin (B, D) at low and high CV (blue solid and orange dashed lines, respectively) for +ESI (A, B) and −ESI (C, D). For lysozyme, different values were chosen for the high CV (e.g., 540 eV in +ESI and 480 eV in −ESI) because these were the last analyzed CV where the signal-to-noise ratio (S/N) for the 6 ± ions was greater than 3." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Anal_Chem_2026_98_6_4518_4527_Figure_2_Representative_mobiligrams_showing_arrival_times_for_lysozyme_A_C_and_a_lactalbumin_B_D_0f3d23c3c1.jpg 212w," sizes="100vw" width="1600" height="1178"></p><p>To characterize the stabilizing effect of disulfides, MD simulations were conducted that heat denatured 6+ ions of lysozyme and α-lactalbumin with disulfide bridges either present or removed with the resulting cysteine residues being protonated prior to heating (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c04295/suppl_file/ac5c04295_si_001.pdf">Figure S4</a>). Structural changes associated with heat denaturation were characterized by taking the root-mean-square deviation (RMSD) of the heated structures relative to initial, crystal structures. Over ten trials, lysozyme ions possessed an average RMSD of (1.6 ± 0.2) nm when disulfides were present which increased to (3.5 ± 0.5) nm when disulfides were removed. Similarly, the RMSD of α-lactalbumin ions increased from (1.8 ± 0.1) nm when disulfides were present to (3.7 ± 0.3) nm when disulfides were removed, suggesting that the disulfides serve as a barrier to unfolding. This is visually represented in <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c04295/suppl_file/ac5c04295_si_001.pdf">Figure S4C,D</a> where simulated structures of heated lysozyme and α-lactalbumin ions with intact disulfides adopt more condensed configurations relative to those with disulfides removed. In essence, the disulfides “tie” disparate regions of protein together, which serves as a barrier to more thorough unfolding even at a maximum simulated temperature of 900 K, explaining the similarity of <sup>TW</sup>CCS<sub>N2→He</sub> values in +ESI versus −ESI as well as the limited percentage of ions that undergo a change in <sup>TW</sup>CCS<sub>N2→He</sub> upon additional collisional activation.</p><p>WGA has 16 disulfide bridges per monomeric subunit (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c04295#tbl1">Table 1</a>). On average, these disulfides encompass seven amino acids each, with ∼78% the total amino acids in WGA being encompassed by at least one disulfide bridge (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c04295/suppl_file/ac5c04295_si_001.pdf">Figure S3</a>). Compared to lysozyme and α-lactalbumin, the presence of disulfide bridges across small numbers of amino acids enables WGA to unfold with ΔCCS of (370 ± 60) Å<sup>2</sup> and (390 ± 120) Å<sup>2</sup> in +ESI and −ESI, respectively (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c04295#tbl2">Table 2</a>). However, in comparison to the other lectins, GNA and con A, we hypothesize that these disulfide bridges in WGA limit the extent of unfolding, resulting in the extended, <sup>TW</sup>CCS<sub>N2→He</sub> values being within experimental uncertainty in both ion modes.</p><p>To summarize, lysozyme and α-lactalbumin exhibit similar gas-phase behavior in both +ESI and −ESI, with most ions retaining folded structures even under high CV. We hypothesize this resistance to unfolding is largely attributed to their four disulfide bridges, which span over 90% of their sequences and act as stabilizing constraints. MD simulations confirm that removing these disulfides significantly increases structural deviation during heat denaturation, indicating their critical role in maintaining compact configurations. Consequently, the presence of disulfide bridges explains the minimal changes in <sup>TW</sup>CCS<sub>N2→He</sub> and the proteins’ high stability under activation.</p><h4><strong>Conclusions</strong></h4><p>IMS-MS allows for detailed analysis of the structure and stability of native-like proteins in the gas phase. The structure of a protein is dictated by its amino acid sequence and the resulting noncovalent interactions that form the secondary, tertiary, and quaternary structures. Chargeable amino acid residues that are solvent exposed can carry charges leading to the protein having a net-positive, net-negative, or net-neutral charge in solution at physiological pH. Yet, most native IMS-MS analysis is conducted in +ESI, leading to proteins that are net-negative in solution experiencing large swings in their net-charge during the ESI process.</p><p>This work highlights that gas-phase stability of native-like proteins varies with ionization polarity. While CCS values for folded structures are generally comparable between +ESI and −ESI, unfolding energetics differ─net-negative proteins are more stable in −ESI, whereas net-positive proteins are more stable in +ESI. We hypothesize that these differences are due to changes in the intramolecular interactions within cationic and anionic proteins. Therefore, proteins analyzed in the mode opposite to their solution-phase charge may have different gas-phase structures compared to biological systems. For example, proteins that are net-negatively charged in physiological environments (pI &lt; 6.5) are more likely to represent their biological counterparts as gas-phase anions when analyzed in −ESI compared to +ESI, enabling nMS experiments to more closely characterize the structures present in biological systems.</p></div>

Investigating the Effect of Isoelectric Points on the Gas-Phase Stability of Native-like Proteins Analyzed in Positive- versus Negative-Ion Mode by IMS-MS

<p><strong>Anna Vanluchene&nbsp;from UCT Prague’s&nbsp;Department of Chemical Engineering has received a&nbsp;prestigious start-up grant from the Dagmar Procházková Fund. However, she did not receive funding right away. In this interview, she describes how she developed ten versions of her&nbsp;</strong><i><strong>Illuminating Flow</strong></i><strong>&nbsp;project idea (combining photocatalysis with flow reactors for pharmaceutical synthesis). She explains why she considers perseverance to be crucial when applying for grants, how international experience has influenced her approach to team management, and how her research can reduce the chemical industry’s&nbsp;dependence on fossil fuels and imports from China.</strong></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/VSCHT_Praha_Na_startovaci_grant_jsem_cekala_dva_roky_a_napsala_deset_verzi_projektu_2_5b7d63b8e9.jpg" alt="VŠCHT Prague/Tomáš Balický: I waited two years for a start-up grant and wrote ten versions of my project idea" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_VSCHT_Praha_Na_startovaci_grant_jsem_cekala_dva_roky_a_napsala_deset_verzi_projektu_2_5b7d63b8e9.jpg 127w," sizes="100vw" width="1128" height="1387"></p><h5><strong>What did the Dagmar Procházková Fund grant mean to you?</strong></h5><p>I&nbsp;consider it to be a&nbsp;great success. It is the first injection of funding that will allow me to ensure full independence for my research endeavour, to start my own research group, and to fund students so I&nbsp;can get started properly.</p><h5><strong>What have been your previous experiences with grants?</strong></h5><p>During my doctorate, a <i>cotutelle</i> (international doctorate under dual supervision), I&nbsp;was funded by a&nbsp;grant from the French government. Then I&nbsp;worked at the Academy of Sciences of the Czech Republic (CAS) and received a&nbsp;Marie Skłodowska-Curie Action (MSCA) Postdoctoral Fellowship to go abroad. The idea for my now-funded project was developed about two years ago and, since then, I&nbsp;have gradually developed and adapted the idea for various grant calls. I&nbsp;submitted about ten different versions of the proposal. I&nbsp;did not receive a&nbsp;grant from the Dagmar Procházková Fund last year, but this year, my application was successful.</p><h5><strong>This probably requires a&nbsp;great deal of patience and perseverance.</strong></h5><p>Certainly, because the success rates for most grants have been declining for some time. But as a&nbsp;motivational example, I&nbsp;will tell the story of Timothy Noel, a&nbsp;Belgian professor of chemistry living in the Netherlands. He applied for the prestigious European Research Council (ERC) grant, which is among the most sought-after in Europe, seven times. But no failure deterred him and eventually he succeeded and opened the door to potentially massive grant funding. He was already one of the world’s&nbsp;top scientists in the field at that time and openly described his journey on his blog <a target="_blank" rel="noopener noreferrer" href="https://www.noelresearchgroup.com/2022/03/17/my-personal-story-to-obtain-an-erc-grant-7-submissions-4-interviews-and-6-heartbreaks/"><strong>blog</strong></a>.</p><h5><strong>What advice does this convey to other grant applicants and early career researchers?</strong></h5><p>Start early, read a&nbsp;lot, don’t&nbsp;give up, and—most importantly—apply repeatedly. Learn from rejections and overcome possible frustration from failures. Read blogs and books by successful people, where you will find not only the glorious results of their work, but also the hardships they faced over their entire journeys. Of course, building your team and laboratory is impossible without finances. I&nbsp;myself still hope that I&nbsp;will be able to receive even bigger grants in the future.</p><h5><strong>How has your international experience influenced your scientific approach?</strong></h5><p>A&nbsp;lot and on several levels. Different laboratories teach you how to do&nbsp;things differently. You gain varied experience about how different institutions function. You see other people’s&nbsp;positive motivations, their ability to be ambitious without negativity, their involvement in institutional matters, their openness to cooperation with companies (e.g., tech transfers, spin-offs). The most important thing is to broaden your horizons. I&nbsp;see going abroad as a&nbsp;necessity. What I&nbsp;have taken away the most is drive, great support, and the idea that scientific output is not just about metrics, but also about dedication to one’s&nbsp;topic.</p><h5><strong>What is your </strong><i><strong>Illuminating Flow: Transport Phenomena in Photocatalysis</strong></i><strong> about, in layperson’s&nbsp;terms, and how is it unique?</strong></h5><p>Most of today’s&nbsp;chemical industry is still based on thermal processes and fossil fuels. Photochemistry enables electrification, where the energy source is photons delivered by LEDs, which can generate electricity from renewable sources. Current research focuses mainly on chemical reactions and their mechanisms, but as a&nbsp;chemical engineer, I&nbsp;focus on designing processes and reactors suitable for industrial use. In batch reactors, light fades rapidly with distance from a&nbsp;source, so much of a&nbsp;reaction mixture is not illuminated. Flow reactors solve this problem, but they bring new challenges such as working with solid catalysts and subsequently scaling up production and achieving higher production rates of the desired chemicals at a&nbsp;given scale.</p><p>One can imagine a&nbsp;transparent tube with a&nbsp;catalyst on the walls, upon which light shines and through which reactants flow. This project has a&nbsp;unique emphasis on engineering solutions and overall process efficiency.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/VSCHT_Praha_Na_startovaci_grant_jsem_cekala_dva_roky_a_napsala_deset_verzi_projektu_3_b978abf25c.jpg" alt="VŠCHT Prague/Tomáš Balický: I waited two years for a start-up grant and wrote ten versions of my project idea" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_VSCHT_Praha_Na_startovaci_grant_jsem_cekala_dva_roky_a_napsala_deset_verzi_projektu_3_b978abf25c.jpg 241w," sizes="100vw" width="1228" height="799"></p><h5><strong>So, were you inspired by a&nbsp;gap in the market to connect photocatalysis with transport phenomena?</strong></h5><p>Exactly. I&nbsp;combine my areas of expertise: microfluidics, photocatalytic degradation of organic substances (CAS), and synthesis (MSCA Postdoctoral Fellowship). The idea itself is not new, and pharmaceutical companies are very interested in “greener” photochemistry, but in practice, there is often a&nbsp;lack of appropriate engineering solutions and apparatus for industrial use.</p><h5><strong>What are the practical applications of your work and what substances are you focusing on?</strong></h5><p>Mainly on pharmaceuticals and on the synthesis of so-called fine chemicals, which are often the building blocks for the production of pharmaceuticals. There is also a&nbsp;geopolitical dimension to this, i.e. less dependence on imports from China and sustainable synthesis in Europe where it makes economic sense.</p><h5><strong>And what chemicals are you specifically talking about?</strong></h5><p>For example, building blocks for advanced synthesis, compounds prepared by trifluoromethylation reactions, or products of oxidation reactions with singlet oxygen. At the same time, we focus on reactions that are, in the classical design process, less safe or technologically demanding, where new approaches, such as photochemistry in flow reactors, could be safer and have better process control. Of course, this is not a&nbsp;universal solution for all types of reactions.</p><h5><strong>The goal of this project?</strong></h5><p>I&nbsp;plan to start a&nbsp;fully functional laboratory and research team, create high-quality experimental data on selected molecules and based on them, try to build cooperation with industrial partners. Without data, it is impossible to come to companies with just an idea. Within three years, I&nbsp;would like to have results that can be realistically presented and further developed.</p><h5><strong>What are the main challenges in transport phenomena during photocatalysis?</strong></h5><p>The methodology for repeatability of experiments in photochemistry is relatively demanding and there are unforeseen obstacles in building apparatus. Also, the scale-up from microliters to a&nbsp;larger scale.</p><h5><strong>What methodology will you use, and how big are the microreactors and their flow rates?</strong></h5><p>I&nbsp;have two different directions in methodological design. The first direction involves microreactors the size of a&nbsp;laboratory slide. You make a&nbsp;structure using a&nbsp;laser, and then you have to cast it and make a&nbsp;microreactor. This allows you to quickly adjust the geometry of the reactor. This method is, of course, not applicable in the commercial setting, but it is ideal for studying transport phenomena and precise measurements.</p><p>The second direction involves reactors that are flow cells. These are already larger, approximately 15 x 15 centimetres, and their flow rates are in the order of millilitres per hour. This is the initial scale that we will further increase during the project.</p><h5><strong>There is a&nbsp;big difference between a&nbsp;flow rate of microlitres per hour and industrial needs. Will it not work differently in reality?</strong></h5><p>Our research will focus on studying the phenomena themselves for now, and scaling will be addressed later. In addition, we will combine the experimental data obtained with computer simulations that will help design suitable conditions for a&nbsp;larger scale. For some high-value fine chemicals, these scales, combined with continuous operation or parallelization of reactors, may already be practically usable.</p><h5><strong>What catalysts will you use and how will you attach them to the reactor walls?</strong></h5><p>I&nbsp;am focusing on heterogeneous photocatalysis, and we will mainly use graphitic carbon nitride and its more advanced modifications. These are semiconductor materials that can be synthesized relatively easily and are suitable for immobilization on glass reactor walls. A&nbsp;key part of this project is the creation of a&nbsp;stable catalytic layer for long-term flow-through operations. To increase the contact of reactants with the catalyst, we will also consider multiphase modes, for example, gas bubbling, in order to disrupt the otherwise laminar flow.</p><h5><strong>Why did you choose this field and the Department of Chemical Engineering?</strong></h5><p>During my postdoc in Belgium, the department had an opening for an Assistant Professor position that caught my attention and I&nbsp;applied for it. I&nbsp;did my undergraduate, graduate, and initial doctoral studies here, and I&nbsp;love the department. I&nbsp;have a&nbsp;Bachelor’s&nbsp;degree in Chemistry.</p><h5><strong>Are you collaborating with anyone?</strong></h5><p>We collaborate with BUT Brno focusing on creating layers and immobilizing catalysts on glass, as well as with the Institute of Chemical Process Fundamentals of the Academy of Sciences of the Czech Republic. And as for organic synthesis, we are connected with Ghent University via postdoc internships. At the same time, my colleague Viola Tokárová and I&nbsp;received a&nbsp;Czech Science Foundation grant in cooperation with BUT Brno and Masaryk University, with our part of the project focusing on the use of flow reactors for photochemical reactions and testing the antibacterial properties of photocatalytic materials. And I&nbsp;am writing other grant proposals in which I&nbsp;am trying to build new collaborations.</p><h5><strong>What does the creation of an independent research group at UCT Prague look like?</strong></h5><p>I&nbsp;started by renovating the premises that were assigned to me and gradually building my team. It is important for research work to have Ph.D. students; I&nbsp;have already hired one and we will recruit more. In addition to building the group, I&nbsp;will engage in securing further funding for the group, so I&nbsp;will be writing more grant proposals. It is important to think far enough in advance when it comes to prospective funding for a&nbsp;research group.</p><h5><strong>What type of students are you looking for?</strong></h5><p>The laboratory and team I&nbsp;are building will be very multidisciplinary, just like the area I&nbsp;am working on. That is why I&nbsp;am looking for students who are attracted to true multidisciplinary research, those who, for example, have knowledge of engineering, but who don’t&nbsp;mind a&nbsp;little bit of pure chemistry. One student in their own right does not have to (and cannot) know every subject, so I&nbsp;will ideally have a&nbsp;team consisting of different people with different research backgrounds. Motivated, DIY-type students who would rather enthusiastically build or invent something themselves than conduct repetitive measurements. Organic or analytical chemists will also find their place here. If this topic is interesting to students in any way, they can definitely contact me. I&nbsp;am also open to interdepartmental cooperation with other UCT Prague Faculties.</p><h5><strong>How would you describe your path to photocatalysis/chemical engineering?</strong></h5><p>Studying Chemistry as an undergrad gave me a&nbsp;broad perspective, but I&nbsp;was gradually narrowing my focus and eventually chose engineering. Chemical engineering intrigued me with its logic and was the easiest for me to grasp at the time. But I&nbsp;have always enjoyed working on projects more than the studies themselves. Even during my Bachelor studies, I&nbsp;really enjoyed and was interested in the Professor Štěpánek Group’s&nbsp;projects, where I&nbsp;was doing something completely different than I&nbsp;do&nbsp;now. I&nbsp;only got into photochemistry during my time at CAS and then, during my postdoctoral fellowship, I&nbsp;devoted myself to electrochemistry. My current focus is, thus, a&nbsp;natural interlinking of all these areas. Consequentially, I&nbsp;developed an awareness of the necessity to become independent and return to the department with my own, different research agenda, which, in my opinion, is an important and correct basis for establishing my own research group.</p><h5><strong>What is the biggest challenge of this project for you?</strong></h5><p>The transition from being a&nbsp;postdoc to a&nbsp;leadership position is a&nbsp;big change for me and I&nbsp;think it is not talked about enough. It means a&nbsp;shift from my own experimental work to leading a&nbsp;team, planning and delegating tasks, and motivating students. From a&nbsp;practical point of view, one of the main challenges is the transfer of reactions from the microscale to functional systems, the construction of reactors, the immobilization of catalysts, and generally confirming that this direction makes sense in the long term and that it has future potential.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/VSCHT_Praha_Na_startovaci_grant_jsem_cekala_dva_roky_a_napsala_deset_verzi_projektu_1_66ac267e06.jpg" alt="VŠCHT Prague/Tomáš Balický: I waited two years for a start-up grant and wrote ten versions of my project idea" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_VSCHT_Praha_Na_startovaci_grant_jsem_cekala_dva_roky_a_napsala_deset_verzi_projektu_1_66ac267e06.jpg 155w," sizes="100vw" width="830" height="839"></p>

I waited two years for a start-up grant and wrote ten versions of my project idea

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The University of Chemistry and Technology, Prague is a natural centre of first-rate study and research in the area of chemistry in Czechia and is one of the country's largest educational and research institutions focused on technical chemistry, chemical and biochemical technologies, material and chemical engineering, food chemistry, and environmental studies.

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<p><strong>In recent years, glucagon-like peptide-1 receptor (GLP-1R) agonists have gained significant attention because of their effectiveness to treat obesity and type 2 diabetes. The global market for GLP-1 analogues is projected to grow rapidly, reaching $260 billion by 2034. Developing sensitive bioanalytical assays to determine pharmacokinetics and toxicokinetics is crucial for advancing these medications.&nbsp;</strong></p><p>Traditionally, the plasma concentration of GLP-1 analogs was measured by ligand binding assay, which requires time to develop antibody and lack selectivity and specificity. Liquid chromatography-mass spectrometry (LC/MS), which is used for sequence identification of GLP-1 receptor agonists, has emerged as an alternative methodology to precise quantify these molecules in biological matrix because of its superior sensitivity, wide dynamic range, and high specificity. Here we present an automated workflow, which combines automation and LC/MS technologies, to quantify GLP-1 analog drug in human plasma by using an Agilent 1290 Infinity II Bio LC and an Agilent 6495D triple quadrupole system (Figure 1). Our results indicate that this automated LC/MS workflow can enhance assay sensitivity by five times compared to traditional organic solvent precipitation.&nbsp;</p><p>This workflow can be used for quantitative analysis of GLP-1 therapeutics without the need to have specific antibody while providing excellent sensitivity, high specificity and fast method development, which will play a crucial role in drug discovery and development.</p><blockquote><p><strong>Presenter: </strong>Xi Qiu, PhD (LC-MS Application Scientist, Agilent Technologies, Inc.)</p><p>Xi Qiu is application scientist at Agilent, he has extensive experience using LC-MS for large molecules analysis including protein, protein conjugates, peptide, and oligos. He earned his Ph.D. degree from the department of Pharmacognosy and Medicinal Chemistry at University of Illinois at Chicago focusing on benefits and safety of botanical dietary supplements and herbal-drug interactions. After graduation, he did his postdoc training at Pfizer and Bristol Myers Squibb where he worked on drug transporters protein expression analysis in tissues as well as drug induced liver injury mechanism. He then worked for two major contract research organizations leading their large molecule LC-MS group performing protein, protein conjugates, peptide, and oligos pharmacokinetics/toxicokinetics analysis under GLP/regulated environment. Prior to joining Agilent, he worked at Johnson and Johnson where he focused on large molecule quantification using LC-MS at intact and peptide level.</p></blockquote>

Agilent Technologies: Comprehensive workflow for Automated Sample Cleanup and Sensitive Quantitation of Glucagon-like peptide-1 (GLP-1) Analogs from Plasma

Comprehensive workflow for Automated Sample Cleanup and Sensitive Quantitation of Glucagon-like peptide-1 (GLP-1) Analogs from Plasma

Discover automated LC/MS approach for GLP-1 bioanalysis with Agilent, delivering higher sensitivity, specificity, and assay development without antibodies.

Automated Sample Cleanup & Sensitive Quantitation of GLP-1

<div><h4><strong>Navigating Challenges and Opportunities for Environmental Testing Labs Under the Revised EU Water Framework Directive</strong></h4><p><strong>The European Commission’s proposed updates to the Water Framework, Groundwater, and Environmental Quality Standards Directives are bringing new responsibilities and opportunities for environmental testing labs. With expanded pollutant lists - including PFAS, pharmaceuticals, and pesticide metabolites - and stricter monitoring and reporting requirements, the landscape of water analysis is rapidly evolving.</strong></p><p>Join the 4th Waters Environmental Webinar Series to explore how your lab can navigate these challenges and turn regulatory change into opportunity.</p><p>Register for free and partner with us to shape the future of European water quality.</p><h5><strong>Why Attend</strong></h5><p>Stay ahead of new EU regulatory demands with insights from leading experts. Gain practical guidance, share experiences with peers, and prepare your lab for the next generation of water quality standards.</p><h5><strong>Highlights</strong></h5><ul><li>New pollutant categories and analytical challenges</li><li>Updates to monitoring protocols and reporting</li><li>Innovative methods to meet revised Environmental Quality Standards</li><li>Strategic guidance for compliance and adaptation</li></ul><p><strong>Lead the change in water analysis—stay ahead, stay compliant, and make a real impact.</strong></p><h4><strong>EPISODE 2: PFAS in the Environment: A Deep Dive into Analysis, Regulation, and Real-World Data</strong></h4><h4><strong>What you Will Learn</strong></h4><ul><li>How to maintain sub-ng/L LOQs in water samples with direct injection</li><li>How an extended number of PFAS and Relevant Potency Factors in the upcoming EU Water Framework Directive can be addressed</li></ul><blockquote><p><strong>Presenter:</strong> Jana Kováčová (PFAS Lead for Continental Europe, ALS Czech Republic)</p><p>Jana Kováčová is an analytical chemist with over 15 years of experience in method development and validation. She earned her MSc and PhD from the University of Chemistry and Technology, Prague (UCT Prague), where she specialized in analytical methods for pesticide residue determination in water and food matrices of both plant and animal origin.</p><p>In 2020, Jana joined ALS Czech Republic as a Validation Specialist within the environmental analytical innovations group, later transitioning to a full-time focus on PFAS (per- and polyfluoroalkyl substances) analytics. In 2022, she was appointed Supervisor of the PFAS Section.</p><p>Currently, Jana serves as the PFAS Lead for Continental Europe. In this role, she coordinates ALS’s PFAS analytical activities across the region, acting as a key technical representative for PFAS topics. She supports laboratories and clients with strategic guidance and data interpretation, aligns testing approaches across multiple sites, and ensures consistent, high-quality delivery. To stay at the forefront of the field, Jana closely monitors legislative updates and emerging trends, sharing her expertise through client webinars, seminars, and presentations at scientific conferences</p><p><strong>Presenter: </strong>Sara Beverly (Principal Sales Application Chemist, Waters)</p><p>In her current position, Sara is a Principal Sales Application Chemist specializing in food and environmental LC-MS/MS based applications within the Waters UK and Ireland demo laboratory. Sara has worked in F&amp;E analysis with various research interests including the development of both multi-residue HRMS screening and targeted LC/GC MS based methods for the past 25 years in both the government and private sectors. Prior to joining Waters Sara was employed as a Lead Scientist at the Food and Environment Research Agency (FERA, Defra, UK) for 14 years. Sara has participated in EU Food and Veterinary Office (FVO) audit inspections, was an expert on behalf of the International Atomic Energy Agency (IAEA) and a member of the EuroResidue conference scientific committee.</p><p><strong>Presenter: </strong>Claudia Rathmann (Principal F&amp;E Market Development Manager, Waters Corporation)</p><p>Experienced and passionate analytical science professional with over 20 years of technical and strategic expertise in food and environmental applications. Currently serving as Principal Market Development Manager at Waters Corporation, Claudia specializes in connecting customers with product management to deliver innovative solutions for complex analytical challenges. With a strong scientific foundation and a proven track record in both technical and marketing roles, Claudia bridges the gap between customer needs and product innovation across the EMEA region.</p></blockquote></div>

PFAS in the Environment: A Deep Dive into Analysis, Regulation, and Real-World Data

Explore PFAS analysis, regulation, and real-world data under the revised EU Water Framework Directive in Episode 2 of the Waters Environmental Webinar Series.

PFAS in Environment: Analysis, Regulation

<p><strong>Join us for Part 1 of our three-part Single-Cell Proteomics Webinar Series, designed to guide researchers through the technologies, workflows, and analytical strategies enabling deeper biological insights at single cell resolution. This introductory session provides a comprehensive overview of the end-to-end workflow and establishes the foundation for the more advanced topics that will follow in subsequent webinars.</strong></p><p>In this session, we will <strong>walk through the complete single-cell proteomics workflow</strong>, from initial sample preparation to liquid chromatography, mass spectrometry, and data analysis. Attendees will see how each component contributes to data quality, sensitivity, and scalability, and how Thermo Fisher Scientific’s integrated portfolio is purpose-built to support high-confidence single-cell protein quantification.</p><h4><strong>Why attend?</strong></h4><p>Participants will gain a clear understanding of:</p><ul><li>How each step in the workflow influences overall data quality and biological interpretation.</li><li>The latest technologies and best practices for generating reproducible, high-sensitivity single-cell proteomics data.</li><li>How Thermo Fisher Scientific’s tools work together seamlessly to deliver actionable insights.</li></ul><p>The session will conclude with a live Q&amp;A, providing participants the opportunity to engage directly with the speaker.</p><p>Whether you are establishing a single-cell proteomics workflow for the first time or looking to optimize an existing platform, this foundational session will equip you with the knowledge needed to navigate the full process with confidence.</p><blockquote><p><span><strong>Presenter:</strong> Bernard Delanghe (Scientific Lead, Proteomics Workflow Applications, Thermo Fisher Scientific)</span></p><p><span>Bernard Delanghe specializes in single-cell proteomics workflows, bringing together advanced mass spectrometry and data analysis approaches. With over 20 years of experience in mass spectrometry and bioinformatics, Bernard is based in Bremen, Germany and has held multiple leadership roles across proteomics hardware and software. He was recognized with the 2018 European Proteomics Association Industry Award for his contributions to Thermo Scientific™ Proteome Discoverer™ software.</span></p></blockquote>

Thermo Fisher Scientific: Single-cell proteomics

Optimizing Every Step: An End-to-End Workflow for High-Confidence Single-Cell Proteomics

Single-cell proteomics webinar: end-to-end workflow from sample prep to LC-MS and data analysis using Thermo Fisher Scientific solutions. Live Q&A included.

Workflow for High-Confidence Single-Cell Proteomics

<p><strong>In Part 2 of our three-part Single-Cell Proteomics Master Class Series, we move beyond foundational workflows to explore real-world applications led by experts actively advancing the field. Featuring Ryan Kelly, PhD (Brigham Young University) and Sarah Sipe, PhD (Parallel Squared Technology Institute), this session highlights how single-cell proteomics is being applied in practice to address complex biological questions.</strong></p><p>Drawing from their own research and facility experience, our guest speakers will share practical case studies, challenges, and strategies for maximizing data quality, throughput, and biological insight—providing attendees with actionable takeaways they can apply immediately.</p><h4><strong>Why attend?</strong></h4><p>Participants will walk away with:</p><ul><li>A clearer picture of real-world challenges and solutions when implementing single-cell proteomics.</li><li>Proven strategies used by experts to maximize data quality, throughput, and interpretation.</li><li>Inspiring examples of how single-cell proteomics is enabling breakthroughs in biology and disease research.</li><li>Practical takeaways that can be applied immediately in your own lab or workflow development.</li><li>An opportunity to engage with the experts in a live Q&amp;A.</li></ul><p>Whether you are preparing to launch a single-cell proteomics program or looking for ways to accelerate ongoing studies, this session provides actionable knowledge from researchers who are already driving innovation in the field.</p><blockquote><p><span><strong>Presenter:</strong> </span>Ryan Kelly, PhD (Professor, Brigham Young University)</p><p>Ryan Kelly is a professor in the Department of Chemistry and Biochemistry at Brigham Young University. His recent research efforts have focused on single-cell and spatial proteomics, which have involved tailoring sample preparation, separations, ionization and mass spectrometry acquisition for low-input samples.</p><p><span><strong>Presenter:</strong>&nbsp;</span>Sarah Sipe, PhD (Head of Mass Spectrometry, Parallel Squared Technology Institute)</p><p>Sarah is a mass spectrometrist with 10 years of experience spanning analysis of primary explosives and drugs to proteins and viruses. Now, Sarah is the Head of Mass Spectrometry at Parallel Squared Technology Institute, where she is pushing the limits of current technologies for total characterization of the single cell proteome.</p><p><strong>Moderator:</strong> Bernard Delanghe (Scientific Lead, Proteomics Workflow Applications, Thermo Fisher Scientific)</p><p>Bernard Delanghe specializes in single-cell proteomics workflows, bringing together advanced mass spectrometry and data analysis approaches. With over 20 years of experience in mass spectrometry and bioinformatics, Bernard is based in Bremen, Germany and has held multiple leadership roles across proteomics hardware and software. He was recognized with the 2018 European Proteomics Association Industry Award for his contributions to Thermo Scientific™ Proteome Discoverer™ software.</p></blockquote>

Real-World Breakthroughs: Expert-Led Applications in Single-Cell Proteomics

Single-cell proteomics webinar Part 2: real-world case studies, expert strategies and practical tips to improve data quality, throughput and biological insight.

Expert-Led Applications in Single-Cell Proteomics

<h4><strong>Food Safety Webinar Series: When Food Meets the Lab</strong></h4><p><strong>Food testing in the region still revolves around “legacy” contaminants that decide release, rejection, and recall discussions - veterinary drug residues, pesticide residues and fumigants, and toxic elements including species-sensitive forms, in different food matrices. This 3-part series is built for audiences where regulatory expectations reference Codex-based frameworks, country-specific legislative guidelines, and import/export-market requirements that influence testing scope, reporting limits, and confirmation criteria. Each webinar focuses on the analytical factors that drive outcomes: matrix effects and co-extractives, trace-level quantitation, transition/ion-ratio checks, interference control, and reportable result logic.</strong></p><p>Keynote expert speakers will set the regulatory context, give a glimpse of the current trends, and future implications. Agilent workflow segments map these needs to sample preparation nuances, LC-MS/MS for multi-class residues, GC-MS/MS and headspace GC for residue/fumigant markers, and ICP-MS plus LC-ICP-MS for heavy metals and speciation, including QC structures and data review patterns used in high-throughput labs, to name a few.</p><h5><strong>Webinar Series Details</strong></h5><ul><li>Register once to attend the complete 3-part series</li><li>Submit your questions beforehand</li><li>Access recorded sessions anytime within one year</li><li>Certificate of attendance will be provided to all attendees</li></ul><h4><strong>Part 1: Veterinary Drugs Edition</strong></h4><p>Veterinary drug residue monitoring increasingly demands broad coverage across classes (β-lactams, sulfonamides, tetracyclines, quinolones, macrolides, nitroimidazoles, chloramphenicol-type compounds and others) at low reporting levels in seafood, dairy and meat matrices. Regulatory context spans Codex-oriented residue frameworks and national controls such as residue provisions under EU and FSSAI, with additional buyer-driven lists and decision rules influencing what labs must report. This session also focuses on the LC-MS/MS methods for multi-class screening and confirmation.</p><blockquote><p><strong>Presenter: </strong>Dr. Niladri Sekhar Chatterjee (Senior Scientist, ICAR-CIFT, Kochi, India)</p><p><strong>Presenter:&nbsp;</strong>Dr. Prasanth Joseph (Application Engineer, LC/MS, Agilent Technologies, India)</p></blockquote>

Agilent Technologies: Food Safety Webinar Series: When Food Meets the Lab

Veterinary Drugs Edition

Veterinary drug residues webinar: LC-MS/MS screening and confirmation in seafood, dairy and meat under Codex, EU and FSSAI regulations.

<p><strong>The end-to-end sample journey represents a structured and traceable pathway that ensures every sample is managed with accuracy, integrity, and compliance from the moment an analysis request is raised to the secure archival of data. This comprehensive approach enables laboratories to deliver reliable results while maintaining operational efficiency and regulatory confidence.</strong></p><h4><strong>Why is this webinar a must‑attend?</strong></h4><p>Join us for this insightful webinar where you’ll explore essential elements of the Digital &amp; Automated Lab, including:</p><ul><li>Efficient management of analysis requests and sample registration, integrated with inventory management.</li><li>Streamlined processes for sample receipt and verification.</li><li>Automation in sample preparation and end‑to‑end sample tracking within chromatography workflows.</li><li>Comprehensive data handling from acquisition and review to reporting, storage, and archiving.</li></ul><p>By overseeing the sample journey from the initial analysis request through to final archival, you ensure complete traceability, stronger data integrity, and improved operational performance. This structured lifecycle not only reinforces compliance and quality standards but also builds stakeholder confidence by guaranteeing that every sample is handled with accuracy and accountability.</p><p>Register now and learn how to turn your scattered digital lab workflows into a connected, holistic, and automated lab ecosystem.</p><blockquote><p><strong>Presenter: </strong>Dr. Nirmal Thakker (Technical Application Support Specialist - Chromatography, Dissolution &amp; Lab Informatics, Agilent Technologies)</p><p>Dr. Nirmal has done his PhD in quality assurance and pharmacy and his master's in pharmacy from the University of Pune. He has more than 15 years of overall industrial experience working in analytical research &amp; development for renowned multinational pharma companies like Glenmark, Torrent, and Piramal. He has also worked with Spinco Biotech as an application specialist for LC. Presently, he is working with Agilent Technologies as a technical application support specialist for chromatography, dissolution, and lab informatics. He has expertise in chromatography, QbD, method transfer, and mass spectrometry.</p><p><strong>Presenter: </strong>Mr. Amit Ghate (Application Specialist - Lab Informatics, Agilent Technologies)</p><p>Amit Ghate is currently working as Lab Informatics Application Specialist at Agilent Technologies. Amit comes from analytical software background where he has an in-depth knowledge of variety of software like Chromatography Data Systems, Data Management, LIMS, Electronic Lab Notebook, databases, reports and Compliance. Prior to joining Agilent, Amit worked with Persistent Systems Ltd as a Project Manager for software support and services. He has done his Masters in Bioinformatics from University of Pune. His main areas of interest is in providing workflow solutions and enabling digital transformation of labs.</p></blockquote>

Agilent Technologies: Automation at the Next Level: Never Lose Track of Your Sample

Automation at the Next Level: Never Lose Track of Your Sample

Webinar on digital lab automation, covering end-to-end sample tracking, chromatography workflows, data integrity, and compliance.

Automation: Never Lose Track of Your Sample

<div><div container-id="cq-colctrl-lt0" comp-id="A1"><div><p><strong>Ion Chromatography (IC) is a critical analytical technique for ensuring drug product safety through accurate and reliable nitrite analysis. This webinar explores how IC is applied across pharmaceutical workflows to quantify nitrite in water, excipients, and finished drug products—supporting effective monitoring and control of nitrosamine impurity risk during manufacturing and storage.</strong></p><p>Attendees will learn how streamlined IC workflows, combined with conductivity, UV-Vis, and mass spectrometry detection, enable sensitive and robust nitrite quantification. The session highlights analytical capabilities, best practices, and practical considerations for implementing IC methods that enhance data confidence, support regulatory compliance, and improve overall product quality.</p><blockquote><p><strong>Presenter: </strong>Chanakya Thaker (Product Applications Specialist, Thermo Fisher Scientific)</p><p>Chanakya Thaker is a Product Applications Scientist within the IC/SP Applications Development team at the Ion Chromatography and Sample Preparation (ICSP) Business Unit, based in Mumbai, India.</p><p>With over 15 years of extensive experience in Ion Chromatography (IC) and Sample Preparation (SP), Chanakya brings deep technical expertise and leadership to his role. He began his career with Dionex, which later became part of Thermo Fisher Scientific, as an Applications Specialist. Over the years, he has successfully advanced into roles that include managing applications teams and overseeing laboratory operations for the IC/SP portfolio at the Center of Excellence in Mumbai.</p><p>He holds a Master of Science in Analytical Chemistry from the University of Mumbai and an MBA in Marketing from ITM Vocational University, Vadodara. In recognition of his contributions to life sciences, he has been awarded an Honorary Doctorate in Life Sciences by the CCU Institute, Florida.</p><p>Chanakya is passionate about advancing analytical technologies, mentoring teams, and driving customer success through innovative solutions. His work continues to support Thermo Fisher Scientific’s mission of enabling customers to make the world healthier, cleaner, and safer.</p><p><strong>Moderator:</strong> Lizzie Gallagher Cagney (Vertical Marketing Manager, Pharma and BioPharma, Thermo Fisher Scientific)</p></blockquote></div></div></div>

Thermo Fisher Scientific: IC Nitrite Analysis: Streamlined Workflows for Reliable Quantification

IC Nitrite Analysis: Streamlined Workflows for Reliable Quantification

This webinar explores how IC is applied across pharmaceutical workflows to quantify nitrite in water, excipients, and finished drug products

IC Nitrite Analysis

<p><strong>Lipid nanoparticle (LNP) payloads are the top choice when it comes to delivering a wide range of nucleic acid therapeutics, like RNA and plasmid DNA (pDNA). But when it comes to characterizing LNPs, assays for size, payload quantification and encapsulation efficiency (EE%) are split up in different steps that slow down any workflow. This split‑assay approach adds complexity, from increased pipetting steps to surfactants that alter pDNA structure and reduce reproducibility and sample throughput. As LNP programs scale up, researchers need simpler, faster LNP characterization in an EE% method that works with any nucleic acid payload.</strong></p><p>In this SelectScience® webinar, Dr. Kevin Lance, Director of Product Management at Unchained Labs, will present new data showing how Stunner AF measures EE% for both RNA‑ and pDNA‑containing LNPs without surfactants, and will demonstrate how avoiding surfactant‑driven particle disruption creates a platform EE% assay that also allows simultaneous reads on size and aggregation from the same measurement. You will learn how to integrate Stunner AF into RNA‑ and pDNA‑LNP screening, formulation optimization, and QC workflows to capture more LNP data in far less time.</p><h4><strong>Key learning objectives:</strong></h4><ul><li>Learn how to characterize size, payload amount, and encapsulation efficiency in a single, one-instrument assay.</li><li>Understand the challenges with pDNA payloads and what steps to take to overcome them.</li><li>Explore the challenges and latest approaches in UV/Vis quantification of LNPs and their payloads.</li><li>Understand how surfactant‑free EE% measurements preserve particle integrity for both RNA‑ and pDNA‑LNPs.</li><li>Learn how to streamline high‑throughput LNP screening with up to 44 samples plus standards on a single 96‑well plate.</li></ul><h4><strong>Who should attend?</strong></h4><ul><li>Formulation and analytical scientists developing and optimizing biologic drug products – including conjugated LNPs, novel formulations, stability studies, excipient screening, and biophysical characterization.</li><li>Process development teams translating early formulations into scalable, manufacturable processes.</li></ul><h4><strong>Certificate of attendance</strong></h4><p>If you attend the live webinar, you will automatically receive a certificate of attendance, including a learning outcomes summary, for continuing education purposes.</p><p>If you view the on-demand webinar, you can request a certificate of attendance by emailing editor@selectscience.net.</p><h4><strong>Webinar details</strong></h4><ul><li><strong>Cost:</strong> Free to attend</li><li><strong>Location:</strong> Online</li><li><strong>Duration: </strong>60 minutes</li></ul><p><i>Registration is required to secure your place. If you register but cannot attend live, you will receive a link to the on‑demand recording once it becomes available.</i></p><blockquote><p><strong>Presenter: </strong>Dr. Kevin Lance (Director, Product Management, Unchained Labs)</p><p>Dr. Kevin Lance covers the Stunner portfolio globally at Unchained Labs. His expertise includes biophysical characterization of proteins, nucleic acids, viral vectors, and LNPs. Prior to Unchained Labs, his research experience covered the fields of sustained antibody delivery and nanotechnology. He earned his Ph.D. in Bioengineering from the joint UC Berkeley – UCSF Bioengineering Graduate Program.&nbsp;</p><p><strong>Moderator: </strong>Olivia Long (Editorial Team, SelectScience)</p></blockquote>

SelectScience: Supercharge LNP EE% and size characterization on Stunner AF

Supercharge LNP EE% and size characterization on Stunner AF

Streamline RNA and pDNA LNP characterization with surfactant-free EE% measurement, size and aggregation in one assay using Stunner AF.

<h4><strong>The Problem</strong></h4><p>Lab automation promises speed and scale, but too often it operates without intelligence. Researchers must translate scientific intent into rigid workflows, scripts, and parameters — requiring deep expertise and constant manual intervention. As experiments grow more complex, automation becomes harder to adapt, forcing scientists to rely on guesswork and slowing iteration.</p><h4><strong>The Solution</strong></h4><p>Stuntman brings native AI into automation to fundamentally change how experiments are run. With built-in intelligence, Stuntman allows researchers to describe their intent in plain language and have experiments designed, executed and analyzed end-to-end. Stuntman creates workflows, runs experiments, logs results, and hands data back for AI-driven interpretation – guiding experiments forward with clarity, adaptability, and purpose.</p><h4><strong>The Proof</strong></h4><p>In this webinar, see how Stuntman turns ideas into executable experiments across pharma, biopharma, materials, energy, consumer goods workflows, and more. Learn how Stuntman’s built-in AI enables experiment design, automated execution and rapid iteration — all on a single, integrated platform.</p><h4><strong>Key Learning Objectives:</strong></h4><ul><li>Understand why traditional lab automation struggles to scale with experimental complexity and where intelligence is missing.</li><li>See how Stuntman embeds native AI into automation workflows to translate scientific intent into executable experiments.</li><li>Learn how a fully integrated platform connects experiment design, execution, data logging, and AI-driven iteration across industries.</li></ul><blockquote><p><strong>Presenter: </strong>Ruja Shrestha (Product Manager, Unchained Labs)</p><p><strong>Presenter:&nbsp;</strong>Sara Kobilka (Contributing Editor, C&amp;EN Media Group)</p></blockquote>

C&EN: Explode into AI-driven Automation with Stuntman

Explode into AI-driven Automation with Stuntman

AI-powered lab automation with Stuntman—design, execute, and iterate experiments end-to-end on one integrated platform.

<h4><strong>Are you interested in automating your NGS workflow but don’t operate a high throughput laboratory?</strong></h4><p><strong>Join our upcoming webinar for an introduction to the Agilent Magnis, a fully automated NGS library preparation instrument that processes up to 8 samples per run with minimal hands on time.</strong></p><p>In the webinar we will share real-life experience using the Agilent Magnis system for automated NGS library preparation in a clinical diagnostics laboratory.</p><p>After a short introduction to the University Hospital Osijek and its molecular testing activities, the talk outlines the clinical and operational context of routine NGS testing. It will highlight the transition from manual to automated workflows, showing how the Magnis system improves efficiency, reproducibility, standardization, and hands-on time.</p><p>Practical diagnostic examples demonstrate how Magnis enables reliable and consistent NGS library preparation under real clinical conditions, offering guidance for laboratories considering automation.</p><h5><strong>What to Expect</strong></h5><ul><li><strong>Product Overview:</strong> Our Product Manager will provide a concise introduction to the Magnis system and its capabilities.</li><li><strong>Real World User Experiences: </strong>Hear directly from customers who have integrated the Magnis into their workflows.&nbsp;</li><li>How a large laboratory in South Africa increased efficiency and reproducibility.</li><li>How a Molecular Pathology lab in Croatia achieved a smooth and confident start in NGS.</li></ul><blockquote><p><strong>Presenter: </strong>Dr. Martin Judex (Channel Partner Manager DGG, Agilent Technologies)</p><p>After studying Biology at the University of Regensburg in Germany, Martin earned his PhD at the University Hospital Regensburg, where he focused on gene expression studies in samples from patients with rheumatoid arthritis. He continued this research as a postdoctoral fellow in San Diego, USA, and later in Munich, Germany, before beginning his sales career at Stratagene.</p><p>When Stratagene was acquired by Agilent, Martin advanced through several sales positions within the company. He currently serves as Channel Partner Manager for Eastern European countries—initially for Genomics, and since 2024 also for Pathology.</p><p><strong>Presenter:&nbsp;</strong>Matt Wang (Product Manager, Agilent Technologies)</p><p>Matt Wang is a Senior Product Manager at Agilent Technologies, where he drives product strategy for next‑generation sequencing (NGS) automation. He leads system architecture and workflow integration for the Magnis NGS Prep System and oversees its global deployment, including expansion into developing markets and OEM partnerships in Greater China. His expertise spans FDA medical device compliance, clinical LDT verification and validation, and integration of LIMS and cybersecurity requirements.</p><p>Matt holds an MBA from the University of California, Irvine, and a bachelor’s degree in Bioengineering from the University of California, San Diego.</p><p><strong>Presenter:&nbsp;</strong>Roberto Pereira, PhD (Senior Field Application Scientist, Diagnostech, South Africa)</p><p>Roberto completed his PhD in Molecular Medicine at the University of the Witwatersrand’s HIV Pathogenesis Research Unit in South Africa, where his research focused on HIV–immune system interactions and HIV vaccine development. His PhD work involved the expression, characterisation and immunogenicity testing of an HIV vaccine immunogen in a non-human primate model. He joined Diagnostech as a Field Application Scientist in 2021, supporting their Pathology portfolio for several years before moving over to the Molecular team to support their NGS customer base. In this role, he continues to grow his expertise in molecular technologies, with a particular focus on next-generation sequencing workflows and applications.</p><p><strong>Presenter:&nbsp;</strong>Jasmina Rajc, MD,PhD (Department Head, Pathology and Forensic medicine, University Hospital Osijek, Croatia)</p><p>Jasminais a specialist in pathological anatomy with extensive clinical and academic experience. She is currently the Head of the Department of Pathology and Forensic Medicine at University Hospital Osijek and an Assistant Professor at the Faculty of Medicine, Josip Juraj Strossmayer University of Osijek in Croatia. Her professional interests include oncopathology, molecular diagnostics, and the evolving role of pathologists in comprehensive genomic profiling. She is actively involved in clinical and scientific research, including national and international studies.</p></blockquote>

Agilent Technologies: Improve Your NGS Workflow With The Magnis

Improve Your NGS Workflow With The Magnis

In the webinar we will share real-life experience using the Agilent Magnis system for automated NGS library preparation in a clinical diagnostics laboratory.

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