🎤Dr. Leigh Terry (University of Alabama)In this episode of Concentrating on Chromatography, we sit down with Dr. Leigh Terry from the University of Alabama to explore one of the biggest challenges in environmental analysis today: understanding—and accurately measuring—PFAS in water systems.While most regulatory methods focus on a small number of compounds like PFOA and PFOS, there may be thousands of PFAS compounds in the environment—and much of that burden goes undetected.<h4>In this episode, we cover:</h4><ul><li>Why PFAS are called “forever chemicals” (and why that label is evolving)</li><li>The limitations of targeted LC-MS/MS methods</li><li>What the fluorine mass balance problem reveals about PFAS destruction</li><li>How combustion ion chromatography (CIC) helps measure total organofluorine</li><li>Why “99.99% removal” doesn’t always mean what you think</li><li>Where PFAS actually end up in wastewater treatment systems</li><li>The most effective technologies for PFAS removal today</li><li>Why drinking water may only account for ~20% of total PFAS exposure</li></ul><h4>Key Insight:</h4>Even when analyzing dozens of PFAS compounds, researchers may only be capturing a small fraction of total organic fluorine—raising major questions about how we monitor and regulate these contaminants.<h3>Video Transcription</h3>In this episode of Concentrating on Chromatography, Dr. Leigh Terry discusses PFAS contamination in drinking water, the analytical challenges associated with measuring these compounds, current treatment technologies, and future directions for monitoring and regulation. The conversation highlights how analytical chemistry, environmental engineering, and public health intersect in addressing one of today's most discussed classes of emerging contaminants.<h4>Understanding PFAS and Their Significance</h4><h5>The University of Alabama Water Quality Research Center</h5>Dr. Leigh Terry is part of the University of Alabama's Center for Water Quality Research. The center operates an analytical laboratory focused on drinking water quality and the detection of contaminants at extremely low concentrations.The laboratory specializes in:<ul><li>Drinking water analysis</li><li>Organic contaminants</li><li>Emerging contaminants</li><li>PFAS monitoring</li><li>Water quality research</li></ul>Their work supports both research initiatives and practical solutions for water utilities and environmental agencies.<h4>Why Focus on PFAS?</h4>Although PFAS compounds have existed since the 1940s, public awareness has increased dramatically only in recent years.According to Dr. Terry, several factors contributed to the rapid growth of PFAS research:<ul><li>Increased media attention</li><li>New regulatory initiatives</li><li>Growing evidence of human exposure</li><li>Expanding research opportunities</li><li>Greater understanding of potential health risks</li></ul>PFAS are not new contaminants. Rather, society is only beginning to understand their prevalence in the environment and their potential impacts on human health.<h4>The Development of Standardized PFAS Methods</h4>One major advancement in PFAS analysis has been the development of standardized EPA methods.These methods allow:<ul><li>Consistent testing procedures</li><li>Comparable results between laboratories</li><li>Regulatory monitoring</li><li>Reliable data interpretation</li></ul>Dr. Terry notes that many of these standardized approaches began appearing around 2018–2019, providing a common framework for analytical laboratories and researchers.<h4>How Large Is the PFAS Universe?</h4>Many people are familiar with PFOA and PFOS, two of the most heavily studied PFAS compounds. However, these represent only a small fraction of the broader PFAS family.PFOA and PFOS are often referred to as:<ul><li>Legacy PFAS compounds</li><li>Original PFAS contaminants</li><li>Early commercial PFAS chemicals</li></ul>The challenge is that even minor modifications to molecular structure create entirely new PFAS compounds.Researchers estimate:<ul><li>Thousands of PFAS compounds exist</li><li>Some estimates exceed 10,000 compounds</li><li>Exact numbers depend on how PFAS are defined</li></ul>Scientific debate continues regarding classification and definition, making precise counting difficult.<h4>Why PFAS Are Called "Forever Chemicals"</h4>Dr. Terry notes that the phrase "forever chemicals" has become widely used, although she suggests the terminology could benefit from rebranding.PFAS persistence results from two key chemical properties.<h5>1. Amphiphilic Structure</h5>PFAS molecules contain:<ul><li>A water-loving (hydrophilic) head group</li><li>A water-repelling (hydrophobic) fluorinated tail</li></ul>This unusual combination allows PFAS to partition between:<ul><li>Water</li><li>Solids</li><li>Air-water interfaces</li><li>Foam</li></ul>Unlike many organic compounds, PFAS can interact effectively with multiple environmental phases.<h5>2. Extremely Strong Carbon–Fluorine Bonds</h5>The carbon–fluorine bond is among the strongest bonds in organic chemistry.As Dr. Terry explains:<ul><li>Large amounts of energy are required to break these bonds</li><li>Natural degradation processes are often ineffective</li><li>Destruction can require highly aggressive treatment conditions</li></ul>These properties make PFAS extremely persistent in both environmental systems and biological organisms.<h4>Toxicity, Regulations, and Environmental Behavior</h4><h5>Understanding PFAS Toxicity</h5>One of the biggest challenges in PFAS regulation is the incomplete understanding of toxicity.Dr. Terry explains that EPA regulations generally consider three factors:<ul><li>Presence in drinking water sources</li><li>Toxicity to humans</li><li>Availability of practical treatment options</li></ul>While some PFAS compounds are known to be harmful, many others remain insufficiently studied. Furthermore, PFAS often occur as mixtures rather than individual compounds.This creates important scientific questions:<ul><li>What is the toxicity of individual PFAS?</li><li>What is the toxicity of PFAS mixtures?</li><li>How should cumulative exposure be evaluated?</li></ul>These uncertainties continue to drive active research.<h4>What Happens to PFAS in Wastewater Treatment Plants?</h4>PFAS do not behave like many conventional contaminants.Rather than remaining fully dissolved in water, they often accumulate at interfaces such as:<ul><li>Water-solid interfaces</li><li>Water-air interfaces</li><li>Foam layers</li><li>Biological solids</li></ul>As a result:<ul><li>Some PFAS accumulate in biosolids</li><li>Some partition into foam</li><li>Some remain in treated effluent</li></ul>Their distribution depends on wastewater composition and treatment processes.<h4>Regulatory Monitoring and Targeted LC-MS Analysis</h4>Current EPA regulations focus on targeted analysis of specific PFAS compounds.Examples include:<ul><li>PFOA</li><li>PFOS</li></ul>Drinking water regulations currently establish maximum contaminant levels (MCLs) for these compounds at extremely low concentrations.Advantages of targeted LC-MS analysis include:<ul><li>Clearly defined analytes</li><li>Established regulatory limits</li><li>High analytical sensitivity</li><li>Reliable quantitation</li></ul>However, limitations remain:<ul><li>Only a small subset of PFAS is measured</li><li>Many PFAS compounds remain undetected</li><li>Total PFAS burden may be underestimated</li></ul>As Dr. Terry notes, targeted analysis provides only part of the overall picture.<h4>The Fluorine Mass Balance Problem</h4>One of the most important concepts discussed in the interview is fluorine mass balance.When PFAS degrade, fluorinated fragments may remain in the environment.This creates a critical question:Are treatment technologies truly destroying PFAS, or merely transforming them into shorter-chain PFAS compounds?To answer this, researchers perform fluorine mass balance calculations using:<ul><li>Targeted PFAS analysis</li><li>Fluoride measurements</li><li>Total organic fluorine measurements</li></ul>A successful destruction process should ultimately convert PFAS into fluoride ions rather than simply producing smaller PFAS molecules.<h4>Advanced Analysis, Treatment Technologies, and Future Directions</h4><h5>Combining Targeted and Bulk Fluorine Measurements</h5>Dr. Terry's group complements targeted LC-MS analysis with measurements of total organic fluorine.Approaches include:<ul><li>Absorbable Organic Fluorine (AOF)</li><li>Extractable Organic Fluorine (EOF)</li><li>Combustion Ion Chromatography (CIC)</li></ul>In these methods:<ul><li>Organic fluorine is captured</li><li>Samples are combusted</li><li>Released fluoride is quantified</li></ul>This provides insight into total fluorinated content, although contributions may originate from sources beyond PFAS, including pharmaceuticals and consumer products.<h4>Surprising Findings from Combined Analysis</h4>One important finding from wastewater studies was that targeted PFAS measurements accounted for only a small fraction of total organic fluorine.Dr. Terry reports that:<ul><li>Approximately 4% of measured AOF could be explained by targeted PFAS compounds</li><li>The majority of organic fluorine remained unidentified</li></ul>This suggests that environmental fluorine chemistry is considerably more complex than currently represented by routine monitoring programs.<h4>Preventing PFAS Contamination in the Laboratory</h4>PFAS analysis requires exceptionally strict quality control.Dr. Terry's laboratory routinely:<ul><li>Tests every new batch of SPE cartridges</li><li>Tests carbon tubes before use</li><li>Uses DI water blanks</li><li>Verifies consumables labeled as PFAS-free</li><li>Collects field blanks</li><li>Monitors analytical blanks throughout workflows</li></ul>These practices help prevent contamination from laboratory materials and consumables, a common challenge in ultra-trace PFAS analysis.<h4>Current PFAS Treatment Technologies</h4>Three technologies currently dominate PFAS removal in drinking water treatment:<ul><li>Granular Activated Carbon (GAC)</li><li>Ion Exchange Resins</li><li>Reverse Osmosis (RO)</li></ul>Selection depends on:<ul><li>PFAS concentration</li><li>Water quality</li><li>Local operating conditions</li><li>Utility infrastructure</li></ul>Although many emerging technologies are being investigated, these remain the most widely implemented solutions.<h4>Membrane Filtration and Pretreatment</h4>Dr. Terry collaborates with colleagues studying membrane-based PFAS treatment.Her own work focuses on pretreatment through biological filtration.The strategy involves:<ul><li>Removing natural organic matter</li><li>Reducing membrane fouling</li><li>Improving membrane performance</li><li>Extending operational efficiency</li></ul>This integrated approach demonstrates how multiple treatment technologies can work together to improve PFAS removal.<h4>Regional Monitoring Projects</h4>The University of Alabama team participates in EPA-supported monitoring efforts along the Gulf Coast.Their observations indicate:<ul><li>PFAS rarely occur alone</li><li>Multiple PFAS compounds frequently co-occur</li><li>Contamination often originates from identifiable point sources</li></ul>Examples include:<ul><li>Industrial facilities</li><li>Manufacturing operations</li><li>Military installations</li><li>Carpet manufacturing facilities</li></ul>Source identification remains a critical component of environmental monitoring programs.<h4>Future Directions for PFAS Monitoring</h4>Looking ahead, Dr. Terry sees several opportunities for improvement.Desired advances include:<ul><li>In situ monitoring technologies</li><li>Portable detection systems</li><li>Reduced analytical complexity</li><li>Lower instrument costs</li><li>Less expensive consumables</li><li>Faster analysis workflows</li></ul>Current PFAS testing requires substantial expertise, specialized instrumentation, and rigorous quality control, making widespread implementation challenging.<h4>Dr. Terry's Perspective on Long-Term Solutions</h4>When asked what major PFAS challenge she would most like to solve, Dr. Terry offered a broader perspective.Rather than focusing solely on remediation, she emphasized prevention.Her view is that society should:<ul><li>Better evaluate chemical toxicity before commercialization</li><li>Assess risks before large-scale deployment</li><li>Reduce introduction of harmful compounds into the environment</li><li>Support utilities tasked with contaminant removal</li></ul>She notes that water utilities often bear the responsibility of removing contaminants they did not create, highlighting the need for broader societal and regulatory support.<h4>Final Thoughts</h4>Dr. Terry encourages consumers to:<ul><li>Learn where their drinking water originates</li><li>Read annual water quality reports</li><li>Stay informed about local water quality</li><li>Consider appropriate home filtration where needed</li></ul>At the same time, she emphasizes confidence in municipal water systems and the importance of continued investment in water quality research, monitoring, and treatment technologies.<h4>Conclusion</h4>PFAS remain one of the most complex challenges in environmental chemistry and water treatment. Through advanced analytical methods such as LC-MS/MS, combustion ion chromatography, fluorine mass balance approaches, and large-scale monitoring programs, researchers like Dr. Leigh Terry are helping improve our understanding of these persistent contaminants.The interview highlights that solving the PFAS challenge will require a combination of better analytical tools, improved treatment technologies, stronger regulatory frameworks, and a greater emphasis on prevention before contaminants enter the environment.<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>

PFAS in Water: Why We’re Missing 96% of the Problem

This study evaluates an immobilized enzyme reactor (IMER) containing peptide N-glycosidase from Rudaea cellulosilytica (PNGase Rc) for rapid online deglycosylation of intact glycoproteins. Human glycoproteins and therapeutic antibodies were used as model substrates to assess reactor performance.The PNGase Rc IMER efficiently removed complex sialylated and core-fucosylated glycans, simplifying protein characterization and glycosylation-site analysis. The approach offers a fast and effective solution for bioanalytical workflows, biopharmaceutical quality control, and stability testing of therapeutic proteins.<blockquote><h4>The original article</h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acsomega.6c00577">Online Deglycosylation of Monomeric Intact Proteins Using the PNGase Rc Immobilized-Enzyme Reactor</a></h4>Katarína Molnárová, Petr Novák, Jana Nováková, and Petr Pompach*ACS Omega 2026, 11, 17, 25724–25729<a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acsomega.6c00577">https://doi.org/10.1021/acsomega.6c00577</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.<div>Protein glycosylation, in which monosaccharide units are attached to a protein backbone through enzymatic pathways, is involved in many important biochemical processes and is considered one of the most important post-translational modifications. <a href="javascript:void(0);">(1)</a> It affects not only the stability and secretion of proteins, cell–cell interactions, and receptor–ligand recognition mechanisms but also the biological activity, plasma half-life, immunogenicity, pharmacodynamics, and pharmacokinetics of biotherapeutics. <a href="javascript:void(0);">(2−5)</a> Therapeutical monoclonal antibodies (mAbs) are among the best known pharmaceuticals that are based on glycoproteins. <a href="javascript:void(0);">(6)</a> Over 90% of the mAbs are derived from immunoglobulin G (IgG), in which N-glycosylation occurs at Asn297 of the Fc region and is responsible for modulating immune responses and interactions with other proteins. <a href="javascript:void(0);">(7,8)</a> In cancer treatment, mAbs are used to increase the response of the immune system against the tumor cell, thus inhibiting the cancerous cell growth and helping with the destruction and elimination. <a href="javascript:void(0);">(9)</a> Among the most commonly used mAbs are trastuzumab, bevacizumab, cetuximab, or margetuximab, which are used as an additional treatment for breast, colorectal, prostate, or lung cancer. <a href="javascript:void(0);">(10)</a>Mass spectrometry (MS)-based methods have become a method of choice in the analysis of mAbs that can provide information on sequence, post-translational modifications, and glycosylation profiles. <a href="javascript:void(0);">(11)</a> The enzymatic removal of the attached glycans from the protein backbone can reduce the complexity of the MS analysis, which can lead to a better understanding of the protein structure and modifications. In glycoproteomics, peptide-N-glycosidase F (PNGase F) is most used for glycan removal. It cleaves the linkage between the Asn residue and the N-acetylglucosamine (GlcNAc). <a href="javascript:void(0);">(12)</a> Jmeian et al. developed a monolithic PNGase F enzyme reactor fabricated in fused silica using a glycidyl methacrylate-co-ethylene dimethacrylate polymer and integrated it into an LC–MS workflow. The authors demonstrated the applicability of this system for the characterization of released neutral and acidic N-glycans by LC–MS analysis. <a href="javascript:void(0);">(13)</a> In another study, oriented immobilization of PNGase F onto a methacrylate-based monolithic support via glutathione-S-transferase–glutathione affinity coupling was employed to release N-glycans from denatured ribonuclease B and fetuin, as well as from native IgG. The released glycans and the corresponding deglycosylated proteins were subsequently analyzed by MALDI-MS. <a href="javascript:void(0);">(14)</a>Gramlich et al. showed the potential of PNGase Rc for N-glycan hydrolysis from both tryptic peptides and native glycoproteins at a low pH. The favorable properties of PNGase Rc, including activity at acidic pH and compatibility with reducing agents such as tris(2-carboxyethyl)phosphine hydrochloride (TCEP) and denaturants like urea, make this enzyme well suited for online intact protein deglycosylation workflows. <a href="javascript:void(0);">(15,16)</a>In this report, we demonstrate the potential of the PNGase Rc IMER for rapid online deglycosylation of reduced monomeric glycoproteins, including human haptoglobin (Hp), human transferrin, anti-hHD6, and the therapeutic monoclonal antibodies trastuzumab and bevacizumab. The column retained its activity over more than 150 consecutive measurements, highlighting its robustness, suitability for repeated use in bioanalytical workflows, and applicability to pharmaceutical research and development.<h4>Experimental Section</h4><h5>Instrumentation and Experimental Conditions</h5>Automated sample handling and online deglycosylation were carried out using the HDX workstation (AffiPro, Czech Republic). The scheme of the system is shown on <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acsomega.6c00577#fig1">Figure 1</a>. Samples of 50 mM ammonium bicarbonate buffer (pH 8.2) and 40 mM TCEP were placed in a sample tray at 4 °C. Ten microliters of the protein sample at a concentration of 0.03 mg/mL (0.3 μg per injection) were added to 40 μL of 50 mM ammonium bicarbonate and then transferred to 50 μL of 40 mM TCEP, pH 2.3. The disulfide bond reduction was carried at 40 °C for 5 min. The automated sample handling system injected 100 μL of the reaction mixture into the sample loop and switched the injection valve. Online deglycosylation was performed at room temperature using a PNGase Rc IMER (2.1 × 20 mm, AffiPro, Czech Republic) at a flow rate of 50 μL/min, followed by protein desalting on an OPTI-TRAP (0.5 × 2 mm) trap column (Optimize Technologies Inc., Oregon City, Oregon, USA) heated to 55 °C for 10 min with 0.2% formic acid delivered by an <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?mainauthorItems=10&amp;search=1260+Infinity+III+isocratic+pump">Agilent 1260 Infinity III isocratic pump</a> (Agilent Technologies, Santa Clara, California, USA). By switching the trap valve, the protein was eluted by an acetonitrile gradient [(min)/% B] 0/10-9/10-16/70-16.5/90-17/90-18/10-23/10] delivered by the <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?mainauthorItems=10&amp;search=1290+Infinity+II+LC">Agilent 1290 Infinity II HPLC</a> system (Agilent Technologies, Santa Clara, California, USA) at a flow rate of 20 μL/min. The mobile phase A consisted of 5% acetonitrile with 1% propan-2-ol and 0.1% formic acid, and the mobile phase B consisted of 95% acetonitrile with 1% propan-2-ol and 0.1% formic acid. The <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?mainauthorItems=8&amp;search=maXis+Q-TOF">maXis Q-TOF mass spectrometer</a> (Bruker Daltonics, Bremen, Germany) was operated in the survey MS mode in a mass range of m/z 50–3000. The acquired data were analyzed and processed by DataAnalysis 4.4 (Bruker Daltonics) and deconvoluted by UniDec <a href="javascript:void(0);">(17)</a> with the following parameters: data processing range, m/z 500–3000; charge range, 1–80; allowed mass range, 1,000–80,000; sampling rate, 10 Da; peak detection range, 500 Da; and peak detection threshold, 0.1.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/ACS_Omega_2026_11_17_25724_25729_Figure_1_Schematic_of_the_automated_sample_handling_system_for_online_protein_deglycosylation_and_desalting_d4ee48b627.jpg" alt="ACS Omega 2026, 11, 17, 25724–25729: Figure 1. Schematic of the automated sample handling system for online protein deglycosylation and desalting. Protein samples, along with 50 mM ammonium bicarbonate and 40 mM TCEP stock solutions were placed in a sample tray chilled to 4 °C, while a second tray heated to 40 °C was used for disulfide bond reduction with TCEP buffer." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_ACS_Omega_2026_11_17_25724_25729_Figure_1_Schematic_of_the_automated_sample_handling_system_for_online_protein_deglycosylation_and_desalting_d4ee48b627.jpg 245w," sizes="100vw" width="1287" height="386"><h4>Results and Discussion</h4>The performance of the PNGase Rc IMER for the removal of complex N-glycans from intact proteins was tested using heavily glycosylated human Hp with four glycosylation sites (Asn184, Asn207, Asn211, and Asn241) <a href="javascript:void(0);">(18)</a> located at the β-chain and occupied by complex N-glycans terminated with sialic acid. Haptoglobin phenotype 2-1, used in this study, forms multimers consisting of β-chain and disulfide linked α1 and α2 chains. <a href="javascript:void(0);">(19)</a> The detection of glycosylated Hp β-chain requires reduction of the disulfide bonds by incubating the protein with a reducing reagent. TCEP is a common reducing reagent used for fast reduction of disulfide bonds at various pH levels. Forty degrees Celsius, the maximum temperature of the PAL tray, and 5 min of incubation were sufficient for complete reduction of Hp disulfide bonds. Individual signals corresponding to the glycosylated β-chain were observed in the m/z range of 35,800–37,400 (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acsomega.6c00577#fig2">Figure 2</a>a). The limited resolution of the mass spectrometer did not allow assigning the different glycoforms of the haptoglobin β-chain, which is occupied by biantennary, triantennary, or tetraantennary glycans with various amounts of sialic acid and fucose. <a href="javascript:void(0);">(20,21)</a> The nonglycosylated α1 and α2 chains were observed at m/z 9190 and 15,940. When the PNGase Rc IMER was integrated into the flow system, a signal at m/z 27,270 was detected, demonstrating complete deglycosylation of the haptoglobin β-chain (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acsomega.6c00577#fig2">Figure 2</a>b).<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/ACS_Omega_2026_11_17_25724_25729_Figure_2_A_Mass_spectrum_of_human_Hp_without_the_PN_Gase_Rc_IMER_implemented_in_the_system_0ecca84ed4.jpg" alt="ACS Omega 2026, 11, 17, 25724–25729: Figure 2. (A) Mass spectrum of human Hp without the PNGase Rc IMER implemented in the system. The base peak signals of the spectrum correspond to both α1 and α2 chains. The signal of the β chain is spread across its different glycoforms. (B) Mass spectrum of human Hp with the PNGase Rc IMER implemented in the system. The signal of the deglycosylated β chain is higher compared to its glycosylated form and observed only at m/z 27,270. This indicates complete removal of glycans from the Hp β chain." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_ACS_Omega_2026_11_17_25724_25729_Figure_2_A_Mass_spectrum_of_human_Hp_without_the_PN_Gase_Rc_IMER_implemented_in_the_system_0ecca84ed4.jpg 245w," sizes="100vw" width="2015" height="913">In a previous study by Krenkova et al., the PNGase F IMER was used for deglycosylation of IgG, RNase B, and bovine fetuin with follow-up mass spectrometry detection of both released glycans and intact proteins using MALDI-TOF MS. <a href="javascript:void(0);">(14)</a> The authors demonstrated an effective method for rapid protein deglycosylation, which, however, requires additional sample handling prior to mass spectrometry measurement. The other study by Jmeian et al., which focused on released N-glycans, implemented a PNGase F IMER with online LC–MS detection. <a href="javascript:void(0);">(13)</a> The authors show the effectiveness of the method by identifying many different glycans released from a single protein or from a complex plasma mixture. Our approach is not directly intended for released N-glycan analysis; instead, it demonstrates the ability to measure intact proteins after rapid online deglycosylation using PNGase Rc at low pH. Samples prepared immediately prior to mass spectrometry analysis using the automated sample-handling platform can reduce variability associated with autosampler residence time, as some proteins may undergo degradation or precipitation during storage in the autosampler.Although all glycoproteins in this study were effectively deglycosylated, the method’s efficiency depends on the characteristics of the individual glycoprotein. Therefore, optimizing method parameters─including the isocratic flow rate, glycoprotein incubation time with TCEP, and/or the addition of denaturing reagent─may improve the overall efficiency of the deglycosylation process.The PNGase Rc IMER stability over a series of injections was tested by using the trastuzumab antibody. The measurements were carried out with the enzyme column kept at the laboratory temperature. As shown in <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acsomega.6c00577#fig5">Figure 5</a>, the results indicate that the column performance remained stable over the course of the 150 measurements, and no glycosylated form of the trastuzumab antibody heavy chain was detected. The activity of PNGase Rc in the presence of 5% acetonitrile and 5% propan-2-ol was evaluated using a bottom-up approach with human 2–1 haptoglobin, which was online-digested by a coimmobilized nepenthesin-2/pepsin IMER. In the absence of an organic solvent, the peptide IEKVVLHPNYSQVD remained fully deglycosylated throughout 30 injections. In contrast, in the presence of organic solvent, a marked loss of enzymatic activity was observed after only a few injections (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acsomega.6c00577/suppl_file/ao6c00577_si_001.pdf">Figure 2</a>).<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/ACS_Omega_2026_11_17_25724_25729_Figure_5_Monitoring_the_stability_and_performance_of_PN_Gase_Rc_IMER_4a9b5a9c53.jpg" alt="ACS Omega 2026, 11, 17, 25724–25729: Figure 5. Monitoring the stability and performance of PNGase Rc IMER. Trastuzumab heavy chain was completely deglycosylated after 150 injections." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_ACS_Omega_2026_11_17_25724_25729_Figure_5_Monitoring_the_stability_and_performance_of_PN_Gase_Rc_IMER_4a9b5a9c53.jpg 170w," sizes="100vw" width="996" height="918"><h4>Conclusions</h4>Here, we demonstrate the potential of the PNGase Rc IMER for the online removal of N-glycans from intact monomeric glycoproteins reduced with TCEP. The column showed high sensitivity toward Hp, which has multiple glycosylation sites with various glycan structures, confirming its suitability for the profiling of complex glycoproteins. Bevacizumab and trastuzumab exhibited similar glycosylation profiles, with core-fucosylated biantennary glycans being the most abundant. Online deglycosylation with the PNGase Rc column resulted in a complete removal of the glycans from the heavy chains of both antibodies, proving that the column can be used for the rapid online deglycosylation of intact therapeutic mAbs. Moreover, the column remained stable over 150 measurements without any loss of activity, even when it was maintained at laboratory temperature. The significantly reduced reaction time, together with full automation and the absence of manual handling steps, substantially improves analytical throughput compared to conventional off-line deglycosylation workflows. These findings highlight the potential of the PNGase Rc IMER in the development of glycoprotein-based biopharmaceuticals, where detailed structural characterization of the protein part is critical for quality control, monitoring batch-to-batch variability, and stability testing.</div>

Online Deglycosylation of Monomeric Intact Proteins Using the PNGase Rc Immobilized-Enzyme Reactor

In the week of June 29, 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 5 500 GC, LC, MS and spectroscopy webinars.</blockquote><h5>1. Thermo Fisher Scientific: Insights from an IC specialist: To be suppressed or not suppressed?</h5><ul><li>Tu, 30.6.2026 09:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6310">Registration</a></li></ul>Join Thermo Fisher’s Ask the Experts session to learn how suppressor technology impacts ion chromatography performance, sensitivity, reliability, maintenance, and troubleshooting.<h5>2. SCIEX: Advancing Proteomics with ZenoTOF: From Single-Cell Analysis to Plasma Biomarker Discovery</h5><ul><li>Tu, 30.6.2026 11:30 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6311">Registration</a></li></ul>Discover how ZenoTOF high-resolution mass spectrometry is accelerating single-cell proteomics and plasma biomarker discovery through enhanced sensitivity, throughput, and automation.<h5>3. Agilent Technologies: Measuring Diverse Samples with UV/VIS Spectrometers and Integrating Spheres</h5><ul><li>Tu, 30.6.2026 20:30 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6052">Registration</a></li></ul>This webinar will discuss diffuse transmission and reflection UV/VIS measurements, including how to perform measurements with Agilent’s Cary 60 UV/VIS Spectrometer.<h5>4. Waters Corporation: Informatics series #33 Tips, Tricks and Best Practices</h5><ul><li>Th, 2.7.2026 11:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6315">Registration</a></li></ul>This interactive session revisits essential features, shortcuts, and practical techniques in Empower software that can streamline everyday laboratory work and reduce unnecessary effort.<h5>5. Waters Corporation: Unlocking Therapeutic Peptide Characterisation (GLP-1RAs) with Cyclic IMS</h5><ul><li>Th, 2.7.2026 15:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6313">Registration</a></li></ul>Discover how cyclic ion mobility spectrometry (cyclic IMS) improves characterization of GLP-1 analogues and therapeutic peptides, supporting development, quality control, and regulatory submissions.<h5>6. Agilent Technologies: Spectral Flow Cytometry Masterclass - Session 1</h5><ul><li>Fr, 3.7.2026 07:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6316">Registration</a></li></ul>Learn how full-spectrum flow cytometry enables high-dimensional cell analysis. Explore spectral flow technology, experimental design, and applications in immunology, oncology, and vaccine research.

Webinars LabRulezLCMS Week 27/2026

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Webinars

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

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

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Don’t miss this exclusive look into how Trilogy Analytical Laboratory, a high-throughput food and feed safety laboratory, relies on robust LC-MS/MS solutions to consistently test for mycotoxins across a multitude of commodities with speed and selectivity.
We’ll look at:
<ul>
<li>How molds and the mycotoxins end up in grain</li>
<li>Differences between testing grain and its byproducts</li>
<li>Improving predictions of mycotoxin occurrence</li>
<li>Delivering trustworthy results to your clients quickly</li>
</ul>
<blockquote>
Presenter: Julie Brunkhorst
</blockquote>
<blockquote>
Julie Brunkhorst has been with Trilogy since it opened in 1999 and is currently the Vice-President of the Technical Division. As an essential part of Trilogy’s growth and success, Julie oversees the daily operations of the laboratory and directs all R&amp;D activities. Her expertise in designing procedures customized for high throughput laboratories has enabled Trilogy to reduce run times, and in many cases, offering same-day turnaround. Julie holds a BAS in Chemistry from Maryville University.
</blockquote>
<blockquote>
Presenter: Carrie Maune
</blockquote>
<blockquote>
Carrie Maune is President and CEO of Trilogy Analytical Laboratory and is one of the original founders of the organization. Carrie has dedicated 23 years of her professional life to helping build Trilogy into the industry-trusted laboratory that it is today. Carrie has 35+ years of mycotoxin experience and has a passion for sharing her knowledge with others. Carrie is a graduate of Central Missouri University.
</blockquote>
<blockquote>
Presenter: Jordon Bierbaum
</blockquote>
<blockquote>
Jordon Bierbaum is the Vice-President of Operations at Trilogy Analytical Laboratory. Jordon started with the organization in 2009 as a chemist and quickly advanced within the laboratory. Jordon has held management positions within Trilogy’s laboratory and production department and this well-rounded experience give him a unique knowledge of quality processes and quality materials. Jordon has his BS of Science in Medicinal Chemistry from the University of Missouri-Columbia and an MBA from Missouri Baptist University.
</blockquote>

SCIEX: The truths, myths, and intricacies of testing mycotoxins

The truths, myths, and intricacies of testing mycotoxins

How Trilogy Analytical Laboratory relies on LC-MS/MS solutions to consistently test for mycotoxins across a multitude of commodities with speed and selectivity.

One declared goal of the EU is that all surface and groundwater bodies achieve good chemical and good ecological status. Pollutants of great concern are regulated within the Water Frame Work Directive 2000/60/EC, amongst them a number of pesticides. The so-called Surface Water Watch Lists help to identify and monitor new substances of concern. On these lists are more and more pharmaceuticals as well as personal care products.
For this reason we developed a multi-residue LC-MS/MS method with the aim to:
<ul>
<li>quantify more than 140 pesticides, pharmaceuticals and personal care products in one run and</li>
<li>reach LOQs of 10 ng/l for all compounds with direct injection of aqueous samples.</li>
</ul>
In this webinar Hannah Willmer will present:
<ul>
<li>What method conditions and instrumentation are needed?</li>
<li>Which are the most challenging compounds?</li>
<li>How does the new waters_connect for Quan software support method development?</li>
</ul>
<blockquote>
Presenter: Hannah Willmer (Senior Applications Chemist, Waters Corporation)
</blockquote>
<blockquote>
Hannah Willmer is an applications chemist in the European demo lab, based in Wilmslow, UK. Her main role focuses on application development work for the food and environmental sector.
</blockquote>
<blockquote>
With a background in bioanalysis supporting the pharmaceutical sector, Hannah further developed a passion for the food and environmental industry. She cultivated this enthusiasm in a contract organization for 6 years where she managed a team and developed methods for the analysis of food and supplements from nutritional testing to food safety compliance. She specialized within the pesticides and contaminants department with a focus on infant formula which brings its own challenges such as more stringent regulations and high throughput.
</blockquote>
<blockquote>
As a former research analyst and Waters client Hannah understands the importance of robust and reliable methods to Waters’ customers and strives to enhance the customers’ experience with the quality comprehensive solutions that are essential to meet the demands in modern testing.
</blockquote>

Waters Corporation: LC-MS/MS Multi-residue Method for Pesticides, Pharmaceuticals and Personal Care Products (PPPCPs) in Water

LC-MS/MS Multi-residue Method for Pesticides, Pharmaceuticals and Personal Care Products (PPPCPs) in Water

What method conditions and instrumentation are needed?; Which are the most challenging compounds?; How does the new waters_connect support method development?

LC-MS/MS Multi-residue Method for Water analysis

LC-MS/MS is rapidly becoming the gold standard for quantifying different classes of analytes in endocrinology research. The power of greater selectivity and analytical sensitivity using LC-MS/MS is critical in understanding the status of endocrine biochemical pathways. The enhanced performance observed on these platforms provides increased confidence in the results, enabling you to make better decisions based on more accurate information.
Greater analytical sensitivity is a goal that drives improvements in precision, leading to clearer insights into results down to low physiological concentrations. Here we will discuss the latest introduction to the Waters MassTrak™ IVD system family, which is shown to be analytically sensitive and efficient, helping to reduce cost and improve the quality of your data. 
Learning objectives: 
<ul>
<li>An introduction to the latest addition to Waters MassTrak IVD System for clinical laboratories
</li>
<li>The importance of selectivity in endocrinology research in obtaining high quality data
</li>
<li>How the latest addition to Waters MassTrak IVD System addresses the needs of those key endocrinology research applications, including steroid hormone analysis
</li>
</ul>
<blockquote>
Presenter: Dominic Foley (Principal Scientist, Waters Corporation)
</blockquote>
<blockquote>
Dominic is a Principal Scientist working at Waters Mass Spectrometry Headquarters in Wilmslow, UK. Having joined the company in September 2013, he has specialized in the development of LC-MS/MS clinical research applications, with expertise in steroid hormone analysis and protein/peptide quantification. In his role, he also collaborates with clinical customers in the development and implementation of LC-MS/MS methods in their laboratories.
</blockquote>
<blockquote>
Dominic has worked in separation sciences for 14 years, following his ambition of improving the quality of healthcare. He started his career with ICON Development Solutions, a CRO in the north of the UK, where he worked as a LC-MS/MS method development and validation scientist supporting DMPK studies in drug discovery. In 2012, he joined Thermo Fisher Scientific to work in their Chromatography R&amp;D team as a Technical Support Specialist, working on the development of new chromatography and sample preparation products.
</blockquote>
<blockquote>
Dominic received his BSc (Hons) in Biochemistry from the University of Manchester in 2006. He has presented his work at conferences around the world and has several publications in both the Microchemical Journal and the Journal of Chromatography A.
</blockquote>
<blockquote>
Presenter: David Ballantyne (Principal Product Manager, Waters Corporation)
</blockquote>
<blockquote>
David Ballantyne is a Principal Product Manager at Waters Corporation, working within the Global Clinical Diagnostics Portfolio Management team. Having joined the company in 2005, he has held multiple roles throughout Manufacturing and R&amp;D. David has a background in Electrical and Mechanical Engineering and began his career at Waters supporting GC-MS/MS technologies including Tandem Quadrupole and Magnetic Sector Mass Spectrometry.
</blockquote>
<blockquote>
In 2018 he moved to his role in Product Management where is focus changed to Clinical Diagnostics, with a particular focus on LC – MS/MS Instrumentation and Informatics solutions. Over the last 5 years David has spent much of his time focused on understanding customer problems and translating them into new solutions.
</blockquote>

Waters Corporation: The Evolving Power of LC-MS/MS Technology within Endocrinology

The Evolving Power of LC-MS/MS Technology within Endocrinology

Here we will discuss the latest introduction to the Waters MassTrak™ IVD system family for clinical laboratories.

The Evolving Power of LC-MS/MS within Endocrinology

This year we invite you to ignite your mind to Be Curious about what Ion chromatography (IC) can do with its versatility in many detections across the IC application spectrum to improve your workflows and solve challenges.
During this three day virtual event, learn from a panel of experts how the latest IC applications are helping colleagues achieve breakthroughs, and walk away with valuable information on how advancements in IC can increase laboratory analytical capabilities. 
Although each day is convenient for a specific region, you can attend any session on any day. All sessions and workshops will be available for on-demand viewing after the event concludes.
<h3>Day 3 Agenda | April 20 | Asia Pacific</h3>
Expand the world of electrochemistry applications and IC hyphenation with high-resolution mass spectrometry and understand how Inductively Coupled Plasma Spectrometry can speciate isotopes while simplifying Pharmacopeia QC analysis and keeping your IC in top-notch condition.
<h5>11:00 AM SGT: Opening Plenary: Electrochemical Detection and Its Application in Ion Chromatography</h5>
<ul>
<li>Yan Liu (Thermo Fisher Scientific, IC/SP R&amp;D, Sunnyvale)</li>
</ul>
<h5>12:00 PM SGT: Application of Anion Chromatography Coupled High-Resolution Mass Spectrometry to Increase Cellular Metabolite Coverage</h5>
<ul>
<li>Vinzenz Hofferek (McConville Lab, Department of Biochemistry and Pharmacology)</li>
</ul>
<h5>1:00 PM SGT: Analysis of Anhydrosugars and Xylooligosaccharides by Ion Chromatography with Electrospray Lithium Cationisation-Triple Quadrupole Tandem Mass Spectrometry</h5>
<ul>
<li>Dr. Estrella Sanz Rodriguez (Natural Products Analysis, Australian Centre for Research on Separation Science (ACROSS), University of Tasmania)</li>
</ul>
<h5>2:00 PM SGT: You Gotta Keep ‘Em Separated: Novel IC Applications for Subsequent Isotopic Analyses by Rapid and/or Hyphenated Techniques</h5>
<ul>
<li>Dr. Brandon Mahan (College of Science and Engineering, James Cook University)</li>
<li>Grace Manestar (IsoTropics PhD Candidate)</li>
</ul>
<h5>3:00 PM SGT: Use of Ion Chromatography in Pharmaceutical Quality Control</h5>
<ul>
<li>Catherine Frankis and Stella Planou (Reading Scientific Services Ltd., Reading Science Centre, Whiteknights Campus)</li>
</ul>
<h5>4:00 PM SGT: Tips on Keeping Your Ion Chromatography in Top-Notch Condition</h5>
<ul>
<li>Ryan Ong (Thermo Fisher Scientific, IC/SP Application Sales Support, Singapore)</li>
</ul>

Thermo Fisher Scientific: IC Symposium 2023

IC Symposium 2023 - Day 3

Join us for the 2023 Global IC Symposium! Day 3 | Asia Pacific.

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

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

How to set MS Scan Parameters for your LCMS Experiment

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

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

Agilent Technologies: How to design an LCMSMS Experiment

How to design an LCMSMS Experiment

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

Targeted workflows are particularly interesting for identifying established biomarkers in various applications. The focus on these workflows, coupled with technological advancements, is continually expanding the boundaries of high-throughput targeted analysis.
<h3>Next Generation of absolute protein Quantitation in Biological Matrixes; higher multiplexicity while faster, robust and sensitive</h3>
<ul>
<li>Presenter: Dr. Christoph Borchers (Mcgill university)</li>
</ul>
The accurate and rapid determination of protein concentrations using multiplexed multiple reaction monitoring (MRM) with isotope-labeled internal standards has the potential to revolutionize biochemistry and medical sciences. The combination of an Evosep One LC with an Agilent QQQ6495C allows a several-fold reduction of analysis time while maintaining high multiplexicity. As an example, we show the use of a multi-protein method for the absolute quantitation of 270 proteins, combined with metabolomics and Artificial Intelligence (AI), to analyze the plasma of a COVID cohort for prediction of survival. Moreover, optimization of the Evosep/6495C combination allowed adaptation of the 270-protein MRM method to a 24-minute gradient, thus doubling the throughput compared to before.
<h3>Development of a LC-MS/MS Method for Measurement of Fusion Sarcoma Proteins in Plasma</h3>
<ul>
<li>Presenter: Phd. AnThony Maus (Clinical Mass Spec. Development Laboratory, Mayo Clinic)</li>
</ul>
Sarcoma is general term for a group of over 70 cancers that are classified using genomic techniques to identify characteristic gene fusions in tumor tissues. However, this technique requires relatively invasive biopsies and is not conducive to monitoring disease progression or response to treatment. Measurements of fusion protein biomarkers in plasma would overcome these limitations. We sought to develop an LC-MS/MS method capable of performing these measurements by conducting discovery experiments on cell lines with an EvoSep coupled to an Exploris 480 mass spectrometer. Using these data, we developed a targeted method and performed measurements in plasma samples.

Targeted Workflows

Targeted workflows are particularly interesting for identifying established biomarkers in various applications.

Targeted LC/MS Workflows

Analysis of PFAS is now an essential part of water testing programs and becoming a regular requirement for monitoring in environment and food sources. As regulations, like Directive 2006/118/EC or Directive 2008/105/EC, continue to be updated, the requirements for method sensitivity have become essential. Solid phase extraction (SPE) is one tool that can be utilized to enhance the sensitivity of a method by enriching the sample, prior to injection. The alternative is to use a direct injection method that relies on the sensitivity of the mass spectrometer.
With the enhanced negative ion sensitivity of the new Xevo™ TQ Absolute mass spectrometer (MS), the boundaries of what is possible for the direct injection of PFAS in environmental samples have been expanded. The high-end MS, in combination with UniSpray; our smart alternative to classic ESI, has been proven to boost the sensitivity especially for PFAS compounds, enhance the ease and simplicity of the direct injection method for PFAS analysis to achieve the high standards of environmental testing labs.
During the webinar, the challenges of ultra-low-level detection of PFAS will be discussed while demonstrating how the latest innovations at Waters could help you overcome them.
<blockquote>
Presenter: Jenny Davies (Principal Applications Chemist, Waters Corporation)
</blockquote>
<blockquote>
Jenny Davies is a Principal Applications Chemist in the European demo lab, based in Wilmslow. Her main role focuses on application development for the food and environmental sector.
</blockquote>
<blockquote>
With a strong background in environmental analysis and more recently working in the food industry. Jenny started her journey nearly 20 years ago in a contract environmental laboratory working in various positions from Laboratory Technician to Technical Director, managing multiple teams and sites. Having worked in many busy laboratories where productivity is paramount, she understands the importance of having robust, simple methods ideal to be carried out efficiently across multiple sites. She specialises in Persistent Organic Pollutants with a focus on environmental samples in soil, water and air.
</blockquote>
<blockquote>
As a former Quality Manager strong Jenny has exceptional understanding of quality and all requirements to adhere to ISO 17025. In addition to this she has been a member of a UKAS Flexible Scope panel in a food laboratory, giving her the knowledge of the different challenges in method development and validation for food commodities. Jenny channels this appreciation for quality into developing comprehensive and compliant applications to solve the challenges in modern testing.
</blockquote>

Waters Corporation: PFAS Analysis - What's possible with unique technologies?

PFAS Analysis - What's possible with unique technologies?

The challenges of ultra-low-level detection of PFAS will be discussed while demonstrating how the latest innovations at Waters could help you overcome them.

Traditional laboratory analysis of the immunosuppressant drugs cyclosporine, everolimus, sirolimus and tacrolimus is well-established in clinical research. However there remains a need for individuals to undergo an invasive, time-consuming and disruptive process under the supervision of trained staff in order to collect a sufficient volume of whole blood for laboratory analysis.
A reliable, remote sampling method may find utility in a clinical research setting. Here we describe the use of Capitainer® B Devices to obtain analytically sensitive, precise and accurate data for cyclosporine, everolimus, sirolimus and tacrolimus analysis using small sample volumes.
Using Capitainer® B devices and very sample small volumes (30 µL of whole blood resulting in a 10 µL dried blood spot), an in-house laboratory method was used on a LC-MS/MS system to meet validation goals for analytical sensitivity, linearity, precision and accuracy for cyclosporine, everolimus, sirolimus and tacrolimus. Furthermore, the advantages conferred by microsampling, notably removing the requirement for travel and a venous blood draw and facilitating home sampling, render this technique applicable to clinical research. 
For Research Use Only. Not for Use in Diagnostic Procedures.
Learning objectives: 
<ul>
<li>Discover how the Xevo TQ Absolute can be used to achieve sufficient analytical sensitivity for a microsampling application</li>
<li>Learn how to achieve fast sample throughput (~2 minute injection-to-injection), minimising time to first result</li>
<li>Explore how MassTrak Immunosuppressant Calibrator and QC Sets can be included in the workflow</li>
</ul>
<blockquote>
Presenter: Stephen Balloch (Senior Scientist, Clinical Scientific Operations, Waters Corporation)
</blockquote>
<blockquote>
Stephen Balloch graduated from the University of York (UK) with a Masters degree in Chemistry which included a strong focus on analytical chemistry and a year in industry, in which he gained experience in a range of analytical techniques.
</blockquote>
<blockquote>
His first permanent post was at Charles River Laboratories, a GLP compliant contract research laboratory in Edinburgh, in which he progressed to the role of Study Director and gained further exposure to LC-MS and LC-MS/MS instrumentation, including Waters instruments.
</blockquote>
<blockquote>
Since 2010, he has been part of the clinical team in the Scientific Operations group in Waters (Wilmslow, UK). His principal focus has been on the development and validation of bioanalytical methods according to CLSI guidelines, with a focus on therapeutic drug monitoring. Additionally, he has supported newborn screening, steroid and vitamin analysis.
</blockquote>

Waters Corporation: Remote Sampling Analysis of Immunosuppressant Drugs with LC-MS/MS

Remote Sampling Analysis of Immunosuppressant Drugs with LC-MS/MS

We will describe the use of Capitainer® B Devices Discover and Xevo TQ Absolute to achieve sufficient analytical sensitivity for a microsampling application.

Remote Sampling of Immunosuppressant Drugs with LC-MS/MS

In Europe, pesticide testing laboratories adhere to the SANTE/ 11312/2021 Guideline. This Guideline ensures a consistent approach controlling the Maximum Residue Levels (MRLs) legally permitted in food or animal feed. Due to the huge number of pesticides of concern, the analysis can be very elaborate, often requiring multiple analytical approaches and laboratory intensive workflows, resulting in high operating costs and slow turn-around times.
In this presentation we describe a comprehensive verified triple quadrupole LC/MS/MS workflow for the simultaneous quantitation of 764 pesticides in tomato adhering to the to SANTE 11312/2021 guidelines. Analytical parameters including limit of detection, linearity, recovery, and precision were evaluated and details of the universal sample preparation procedure and workflow instrumentation configuration will be discussed.
What you will learn
1. How dynamic MRM scheduling allows 764 pesticides to be determined in a single LC/MS/MS run
2. How sample preparation can influence quantitation results
3. How sample preparation, analytical instrumentation and data processing software increases the efficiency of wide-scope pesticide analysis
<blockquote>
Presenter: Peter Kornas (Peter Kornas, Agilent Technologies, Waldbronn, Germany, Agilent Technologies)
</blockquote>
<blockquote>
Peter Kornas has over a decade of experience in the field of development and validation of analytical methods for pesticide, mycotoxin and contaminant analysis using liquid chromatography mass spectrometry (LC/MS). Prior to joining Agilent Technologies as an LC/MS Application Engineer in 2018, he worked as analytical chemist in the food industry working in close cooperation with regulatory affairs to guarantee the fulfillment of legal requirements.
</blockquote>

Agilent Technologies: Quantitative Analysis of 764 Pesticides in Tomato by LC/MS/MS

Quantitative analysis of 764 pesticides in tomato by LC/MS/MS

A comprehensive verified LC/QQQ workflow for the simultaneous quantitation of 764 pesticides in tomato adhering to the to SANTE 11312/2021 guidelines.

LCMS webinars focusing on LC/QQQ - page 26