🎤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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As oligonucleotide therapeutics rapidly emerge as a transformative class of medicines, ensuring their quality and safety has become more critical than ever. In this webinar, Xiaolei Zhuang from the United States Pharmacopeia (USP) will discuss challenges in oligonucleotide quality assessment and USP’s solutions to support reliable analysis. Dr. Bala Addepalli from Waters will explore how tunable enzymes and streamlined informatics enable precise sequencing of mRNA and associated impurities—all within a single LC-MS run.Key Learning Objectives<ul><li>Gain insights into overcoming analytical challenges in oligonucleotide therapeutics</li><li>Discover USP’s products and solutions that enhance quality and consistency</li><li>Explore comprehensive tools to streamline and automate oligonucleotide sequence confirmation, ensuring robust mapping workflows for routine RNA analysis in a GMP environment</li></ul>Who Should Attend<ul><li>Analytical scientists involved in oligonucleotide analysis</li></ul><blockquote>Presenter: Xiaolei Zhuang (Principal Scientist, Global Biologics, US Pharmacopeia)Xiaolei Zhuang is a Principal Scientist in Global Biologics at USP, where she leads the development of reference standards for mAb, insulin, endotoxin and other biologic products. She brings extensive expertise in analytical development, with a strong emphasis on bioassays. Prior to joining USP, she worked in the biopharmaceutical industry, supporting the development of biological therapeutics through analytical, preclinical, and clinical studies, with a focus on CMC components.Presenter:&nbsp;Dr Bala Addepalli, Ph.D., (Director R&amp;D, Waters Corporation)Dr. Bala Addepalli has an impressive background in the field of cell and gene therapy product analysis. Currently, he is the Director of the Evaluations and Application Science Team under the Genetic Medicine analysis portfolio at Waters Corporation. His work focuses on developing efficient analytical approaches for characterization of DNA, RNA, LNPs(lipid nanoparticles), and viral vectors using liquid chromatography coupled with mass spectrometry or light scattering techniques. Before joining Waters, Bala made significant contributions at the University of Cincinnati, where he developed novel enzymes and analytical methods for RNA characterization. His earlier work includes research on mRNA polyadenylation at the University of Kentucky, and viral RNA characterization during his graduate studies in India. With over 60 publications and numerous presentations at scientific meetings, Bala's expertise is well-recognized in the scientific community.Moderated by: Samuel Seal (Biopharma Market Development Manager, Waters Corporation)Samuel Seal is a market development manager specializing in the biologics space. He loves LC and MS – especially on how this technology provides benefit and value.Sam joined Waters in January of 2014 as a Sales Technical Support Specialist in the Irvine office/lab. As a TSS he performed demonstrations on various instruments, provided training for customers, often presented on technical information at varying events, and assisted with troubleshooting from Colorado to Los Angeles. He previously worked at Pyxant Labs in Colorado Springs, CO where he gained extensive experience developing and validating methods for small/large molecules in bioanalytical assays, agricultural commodities, registration of pesticides, and worker exposure studies. He also has experience in column chromatography, sample extraction, sample clean-up, reporting and data management. Sam has hands on experience with running and maintaining various manufacturers' LC/MS/MS systems. Prior to Pyxant, Sam was a Laboratory Instructor at the University of Colorado at Colorado Springs where he earned his Bachelor of Arts in Biology and Bachelor of Arts in Chemistry.</blockquote>

Waters Corporation: Solving Problems That Matter - a Waters webinar series featuring USP speakers

Oligonucleotides

Explore oligonucleotide QC and mRNA sequencing using LC-MS. Hear from USP and Waters experts on challenges and analytical innovations.

<h4>Preparing for next generation LC-MS based proteomics</h4>Presenter: Nicolai Bache (VP Proteomics research at Evosep)

Evosep Biosystems: Preparing for next generation LC-MS based proteomics

Preparing for next generation LC-MS based proteomics

Get a sneak peek of what’s coming at ASMS 2025.

<h4>An introduction to accurate mass and Quadrupole-Time-of-Flight technology with SCIEX</h4>Until recently, nominal mass triple quadrupole technology was considered the gold standard for quantitative assays. In contrast, high-resolution mass spectrometry was primarily used for qualitative, semi-quantitative, and non-targeted workflows, such as metabolite identification, screening, and X-Omics. However, advancements in technology, including faster scan speeds and improved ion optics, have expanded the capabilities of high-resolution spectrometry. Now, it can be effectively applied to both qualitative and quantitative workflows.&nbsp;The ZenoTOF 7600 system, with its high scan rates and enhanced duty cycle at the MS2 level, bridges the gap between these approaches, offering a greater return on investment by reducing data acquisition times and maintaining sensitivity without compromising data quality. This webinar series will focus on how to transition from the Triple Quad to a high-resolution environment for different applications.This webinar series will contain 3 parts. Each part will be 20 minutes with a 10 minute Q&amp;A.<h4>Part 2: Advantages of HRMS for Quantitative Workflows</h4><ul><li>Efficiency and Cost Savings: Discover how HRMS quantitation can significantly reduce time and expenses</li><li>Seamless Transition: Learn the steps to transition your established MRM assays to MRMHR with ease</li><li>Streamlined Processes: Explore methods to streamline the entire workflow from biomarker discovery to quantitation&nbsp;</li></ul><blockquote>Presenter: Heather Chassaing (Senior Accurate Mass Workflow Specialist, SCIEX)Heather Chassaing has over 20 years of experience in analytical science, with a strong background in biochemistry. She has worked extensively in both the agrochemical and pharmaceutical industries, gaining comprehensive expertise in the research and development of drug entities, as well as the complexities of drug production. Heather is particularly passionate about structural elucidation and the application of Mass Spectrometry to these workflows.</blockquote>

SCIEX: An introduction to accurate mass and Quadrupole-Time-of-Flight technology with SCIEX

Advantages of HRMS for Quantitative Workflows

Discover how HRMS quantitation can significantly reduce time and expenses and how to transition your established MRM assays to MRMHR with ease.

<h4>An introduction to accurate mass and Quadrupole-Time-of-Flight technology with SCIEX</h4>Until recently, nominal mass triple quadrupole technology was considered the gold standard for quantitative assays. In contrast, high-resolution mass spectrometry was primarily used for qualitative, semi-quantitative, and non-targeted workflows, such as metabolite identification, screening, and X-Omics. However, advancements in technology, including faster scan speeds and improved ion optics, have expanded the capabilities of high-resolution spectrometry. Now, it can be effectively applied to both qualitative and quantitative workflows.&nbsp;The ZenoTOF 7600 system, with its high scan rates and enhanced duty cycle at the MS2 level, bridges the gap between these approaches, offering a greater return on investment by reducing data acquisition times and maintaining sensitivity without compromising data quality. This webinar series will focus on how to transition from the Triple Quad to a high-resolution environment for different applications.This webinar series will contain 3 parts. Each part will be 20 minutes with a 10 minute Q&amp;A.<h4>Part 3: Alternative Fragmentation Modes – EAD, CID and more</h4><ul><li>What are EAD &amp; other alternative fragmentation modes and how to do they work?</li><li>What do EAD spectra look like for different molecule types?</li><li>Benefits of EAD and when to use it with or instead of CID</li></ul><blockquote>Presenter: Tom Ruane (Accurate Mass Workflows Specialist, SCIEX)Tom has been working for SCIEX since 2018, having worked at Phenomenex since leaving the University of Manchester in 2015. He currently helps SCIEXs customers across Nordic countries, UK and Ireland working in life science research and drug development. In particular he has an interest in accurate mass technologies.</blockquote>

Alternative Fragmentation Modes – EAD, CID and more 

Join SCIEX specialists and learn what are EAD & other alternative fragmentation modes and how to do they work.

Alternative Fragmentation Modes – EAD, CID and more

<div>Eicosanoids and other oxylipins are oxygenation products from polyunsaturated fatty acids. Several oxylipins are highly potent lipid mediators, and many are discussed as biomarkers for diseases. Oxylipin analysis is analytically challenging due to their low abundance and rapid metabolism. Both chromatography and MS/MS are needed because of the presence of closely eluting isomers and similar fragmentation patterns of the molecules. The quantitation is based on external calibration using authentic (isotope-labeled) standards and a sound sample preparation strategy.The webinar explains how to start method development for oxylipin analysis on an LC coupled to a triple quadrupole (QqQ) MS instrument and a high-resolution mass spectrometer (QTof). What is needed, which parameters can be chosen as a starting point, and where can resources/information, e.g., an SOP for sample preparation or calibration, be found?The second part will focus on what is required to characterize the method. This is particularly important when the method is used in publications. Examples of “reporting criteria” recently published as “good practice” by the lipidomics community (https://doi.org/10.5281/zenodo.15044739) will be discussed.The accurate and precise quantitation of oxylipins is then shown for human blood and cells following supplementation with long-chain n3-PUFA. Using these examples, a major limitation of current LC-MS analysis is illustrated: The lack of separation of configuration isomers, i.e. enantiomers, by reversed-phase chromatography. This can be addressed with two-dimensional LC separation: By multiple heart-cutting, peaks are collected following reversed-phase separation and transferred onto a chiral column. Based on the analysis of blood samples, we highlight that the stereo configuration of many oxylipins should only be stated when an enantioselective separation was carried out.<h5>Key Learnings:</h5><ul><li>Method development for oxylipin analysis by LC-MS/MS</li><li>Good practices for method characterization in lipidomics</li><li>Overcoming challenges in oxylipin quantitation</li></ul><h5>Who should attend:</h5><ul><li>Life science researchers looking to enhance their understanding of oxylipin analysis &nbsp;</li></ul><blockquote>Presenter: Nils Helge Schebb (Prof. Dr., University of Wuppertal)Presenter: Paul RS Baker (Sr. Staff Scientific Liaison, Lipidomics and Metabolomics, SCIEX)Presenter: Nadja Kampschulte (Dr., University of Wuppertal)Editor: Christene Smith</blockquote></div>

Wiley: State of the Art Oxylipin Analysis and New Developments

State of the Art Oxylipin Analysis and New Developments

The webinar explains how to start method development for oxylipin analysis on an LC coupled to QqQ and a HRMS QTof

Oxylipin Analysis and New Developments

<h4>Overview</h4>This webinar, co-hosted by Phenomenex and the Bio-Analytical Separation Science Group at Vrije Universiteit Brussel, will cover:<ul><li>The growing potential of oligonucleotide therapeutics and the importance of thorough impurity profiling.</li><li>Challenges in detecting critical impurities such as shortmers and phosphodiesters (PO) during synthesis.</li><li>Ion-pair reversed-phase liquid chromatography’s (IP-RPLC) mechanism of action for high-resolution impurity analysis.</li><li>Evaluating the impact of column preheaters on analyte dispersion and method performance.</li><li>The role of fluoroalcohols in enhancing LC separation and MS detection.</li><li>Comparing bio-inert columns for improved impurity profiling outcomes.</li></ul><h4>Key Learning Points</h4><ul><li>Understand the therapeutic mechanisms of oligonucleotides and the significance of base, ribose, and phosphate modifications.</li><li>Recognize the analytical challenges in oligonucleotide impurity profiling, including shortmers and phosphodiester impurities.</li><li>Learn how to develop and optimize IP-RPLC-MS methods for high-throughput analysis.</li><li>Evaluate the influence of preheater effects and fluoroalcohols on separation and detection sensitivity.</li><li>Compare the performance of bio-inert columns for impurity profiling.</li></ul><h4>Who Should Attend</h4><ul><li>Oligonucleotide Researchers: Ideal for scientists involved in developing and characterizing oligonucleotide therapeutics.</li><li>Analytical Chemists: Professionals focused on impurity profiling and method optimization using advanced chromatographic techniques.</li><li>Biopharmaceutical Quality Control Experts: Valuable for those ensuring the purity, stability, and safety of oligonucleotide-based therapeutics.</li><li>Contract Research Organizations</li><li>Biopharmaceutical Innovator Companies</li></ul><blockquote>Speaker: Dr. Sebastiaan Eeltink &nbsp;(Professor and lead investigator of the Eeltink Laboratory at the University of Brussel &amp; Editor of Analytical Science Advances at Wiley)Dr. Sebastiaan Eeltink is a Full Professor and lead investigator of the Eeltink Laboratory at the University of Brussel and an Editor of Analytical Science Advances at Wiley. His team focuses on developing and designing novel analytics for the high-resolution profiling of biomolecules and biomolecular interactions using ultrahigh-pressure liquid chromatography (UHPLC) and multi-dimensional liquid chromatographic workflows with mass spectrometry (MS) detection. In addition, his team also manages the University’s proteomics platform which offers high-performance LC-MS proteomics profiling expertise and advise to academic and industrial collaborators.Speaker: Quang-Dong Bui &nbsp;(PhD student at University of Brussels)Quang-Dong Bui is currently a PhD student at University of Brussels under the supervision of Professor Sebastiaan Eeltink, where he develops analytical methods for key oligonucleotide projects and is an active scientist in the oligonucleotide and mRNA research community.</blockquote>

Phenomenex: Advanced IP-RPLC-MS Strategies for High-Resolution Oligonucleotide Impurity Profiling

Advanced IP-RPLC-MS Strategies for High-Resolution Oligonucleotide Impurity Profiling

Discover advanced IP-RPLC-MS methods for high-resolution oligonucleotide impurity analysis. Enhance your analytical workflows and data precision.​

Advanced IP-RPLC-MS for Oligonucleotide Profiling

<div><div container-id="cq-colctrl-lt0" comp-id="A1"><div><h4>Lessons learned in developing an ion pair free, compliant workflow for ASO RNA impurity analysis</h4>Join this live webinar with Dr. Ken Cook and discover innovative techniques for oligonucleotide impurity quantitation, automation, and data handling to enhance your laboratory's efficiency and compliance.<h5>Topics:</h5><ul><li>Ion pair free separation mechanisms<ul><li>Reasons for choosing the best path for quantitative methods.</li></ul></li><li>Removing problems of adducts and in-source induced impurities<ul><li>Preventing accurate quantitation of real impurities.</li></ul></li><li>Choice of the best charge states to use for quantitation</li><li>Deconvolution and XIC Component Tables in Thermo Scientific Chromeleon Software<ul><li>Compliant data handling and complementary techniques.</li></ul></li><li>Automation of Annotation, Integration, and Compliant Reporting<ul><li>UV and MS data handling to remove bottlenecks in developing and running new quantitative methods for oligonucleotide impurity analysis</li></ul></li></ul>After the presentation, we planned time to answer your questions.<h5>Who should attend?</h5><ul><li>Laboratory managers or analysts<ul><li>developing methods for new synthetic therapeutic oligonucleotides</li><li>implementing methods for existing modalities</li></ul></li><li>Laboratories<ul><li>involved in clinical trial analysis</li><li>aiming to avoid ion pair contamination in their LC-MS systems</li></ul></li><li>Oligonucleotide analysts in R&amp;D or QC departments</li><li>Analysts looking for green oligonucleotide chemistry</li></ul>You cannot attend the live broadcast on May 22? Please register to automatically receive an email with the link to the recording.<blockquote>Presenter: Dr. Ken Cook (Applications Scientists Manager, Thermo Fisher Scientific)Moved to industry from a University lectureship in Biochemistry, University of Newcastle upon Tyne, following 7 years’ experience in academia. Now with over 35 years’ experience with Thermo Fisher Scientific using a wide range of analytical equipment and software. Publications range from metabolomics, proteomics to large biopharmaceutical drug analysis. Current job title is the European manager for the BioPharma expert support group. This involves the support of Bio-Pharmaceutical applications to characterise protein and oligonucleotide based bio-therapeutics. This involves ongoing collaborations with the Biopharmaceutical industry and academia. Characterization methods of Bio-therapeutics include, monoclonal antibodies, peptides, AAV analytical development, small and large RNA analysis including sequence mapping of mRNA by LC/HRMS.</blockquote></div></div></div>

Thermo Fisher Scientific: ASO RNA impurity analysis

ASO RNA impurity analysis

Discover innovative techniques for oligonucleotide impurity quantitation, automation, and data handling to enhance your laboratory's efficiency and compliance.

<h4>Overview</h4>Participants will gather knowledge of purification and impurity profiling approaches for GLP-1 analogue therapeutic peptides, including size exclusion assessment of peptide aggregates.<h4>Key Learning Points</h4><ul><li>Walkthrough an introduction to Glucagon-Like-Peptide-1 (GLP-1) Analogues</li><li>Learn about stationary Phase Selection and Column Recommendations</li><li>Understand purification and Impurity Profiling Case Studies</li><li>Review am Aggregate Analysis Case Study, and enrichment from Biological Matrices&nbsp;</li></ul><h4>Who Should Attend</h4><ul><li>Any LC users wanting to deepen their knowledge of a set of approaches for the successful purification and analysis of therapeutic peptides.</li></ul><blockquote>Speaker: Lucia Geis Asteggiante (Senior Technical Specialist, Phenomenex)Lucia is a Senior Technical Specialist that has recently joined Phenomenex’s Global Technical Team. She has a broad experience in the field of Analytical Chemistry with a particular focus on LC chromatography coupled with mass spectrometry. Lucia comes from a strong academic and regulatory background with experiences ranging from method development and analysis of small molecules to large protein complexes. She gained her Ph.D. at the University of Maryland - College Park, USA and did her post-doctoral work at the University of Oxford, UK. During her time as a researcher, she has authored/co-authored 23 scientific publications and 2 book chapters.</blockquote>

Phenomenex: Analysis of Glucagon-Like-Peptide-1 (GLP-1) Analogues

Analysis of Glucagon-Like-Peptide-1 (GLP-1) Analogues

Discover strategies for GLP-1 analogue analysis. Enhance your peptide quantification methods with expert tips and best practices.​

Synthetic peptides have emerged as a significant class of therapeutic agents, particularly in the management of metabolic disorders such as type 2 diabetes mellitus. Among these, glucagon-like peptide-1 (GLP-1) receptor agonists have gained prominence due to their multifaceted role in glucose regulation and weight management. Over the past decade, we have witnessed a rise in approvals for these molecules, and the generics market is gearing up as some of these drugs approach patent expiration.Due to the diverse amino acid sequences and structural complexities, synthetic peptides require robust and precise analytical methods to ensure their quality, efficacy, and safety. However, the lack of harmonized regulatory guidelines for peptide characterization presents significant challenges. Certain critical quality attributes (CQAs) are widely accepted among the peptide community, necessitating sophisticated analytical techniques.Given the ongoing speculation in the market regarding the best analytical techniques for synthetic peptides, we are hosting this event to provide a platform for analytical users and chemists working with peptides to ask their queries directly to experts like yourself.Don’t let workflow challenges slow you down. Join us to unlock the full potential of your workflows, enhance your technical skills, and take a significant step in your professional development.<blockquote>Presenter: Dr. Vasanthakumar G. Ramu (Vice President – Head R&amp;D, Peptides and Complex API’s, Alembic Pharmaceutical Ltd.)Dr. Vasanthakumar Ramu, is one of the pragmatic scientists in the pharma industry working around complex API’s. He studied chemical biology from Bangalore University and Indian Institute of Science. In early 2007, hemoved to Max-Planck Institute of Molecular Physiology to work on peptide decorated supramolecular architectures as modulators to study cell protein interactions. Continued further studies as research scientist in Ruhr Universität Bochum, Germany, with the objective to work on backbone modified peptides of HIV protease inhibitors. In 2011 spring, moved to Spain, where he was working as Marie Curie Experienced Researcher to develop Kyotorphin derived peptides, antimicrobial peptides, and other small molecules for neurodegeneration. Returned to India in 2012 and led the startup company called Omgene Life Sciences Pvt. Ltd. Before joining Alembic, was heading peptide process development groups in Biocon Ltd., and Aurobindo Pharma Ltd., Transferred the technologies, successfully validated and filed various DMF’s and involved in commercialization of API’s.Presenter: Dr. Rakesh Shekhawat (Founder/Owner, Proantek Research Labs Pvt. Ltd)Dr. Rakesh Shekhawat is a distinguished scientist with over 20 years of industrial research experience in the fields of synthetic peptides, biosimilars, and oligonucleotide characterization. Holding a Ph.D. in analytical chemistry, Dr. Shekhawat has led analytical research teams at prominent companies such as Intas and USV, contributed significantly to securing various regulatory approvals for biosimilars and synthetic peptides. Recently, he founded Proantek Research Labs Pvt. Ltd., a company dedicated to the advanced characterization of biosimilars, synthetic peptides, and oligonucleotides.Presenter: Dr. Vadi Bhat (Sales Development Manager - Biopharma, Agilent Technologies)Vadi Bhat, Ph.D., is a seasoned biopharma business development manager at Agilent Technologies in India, bringing extensive expertise in biopharmaceutical research and development. He holds a Ph.D. in chemical biology from JNCASR/IISc and completed postdoctoral research at MIT. Dr. Bhat's career includes experience in mass spectrometry core facility management at Baylor Scott &amp; White Hospital/Texas A&amp;M University.Since joining Agilent in 2008, he has played a key role in developing innovative LC-MS workflows for proteomics and biopharma applications, initially at Agilent's Little Falls Center of Excellence in Delaware. From 2015 to 2017, he served as a proteomics market specialist within Agilent's North America Field Team, driving customer collaborations and business development. Transitioning to his current role in India in 2017, he focuses on fostering collaborations and driving business growth in the biopharma sector. Dr. Bhat's contributions to the field are reflected in numerous peer-reviewed publications and presentations at scientific conferences. In 2023, he was appointed adjunct professor at the Manipal Centre for Biotherapeutics Research (MCBR), MAHE, further demonstrating his dedication to advancing biopharma research.Presenter: Dr. Ashish Pargaonkar (Biopharma Workflow Commercialization Lead, Agilent Technologies)Dr. Ashish Pargaonkar is a Lead for Biopharma Workflow Commercialization team for India and also Manager for Centre of Excellences at Bangalore. A Microbiologist by education with a Ph.D, he holds more than 20 years of experience for Biopharma market applications on Hi Resolution Mass Spectrometry. He has a long record of successful demonstrations and customer engagements on workflows for CQA’s, Intact mass, peptide mapping, HCP and Glycans using Agilent state-of-the art solutions. He has authored ASMS posters on media components and therapeutic peptides. Dr. Ashish has been invited speaker at several conferences and workshops at Biosimilar Congress, ADC 2018, IIT (Mumbai, Delhi), ICT (Mumbai), PSI events.Presenter: Dr. Sunil B Lakhmapure (Technical Support Specialist, Agilent Technologies India Pvt. Ltd.)Sunil holds 19 year plus experience in the analytical field with major exposure to LC/GC with Single Quad, Triple Quad and high resolution (QToF) mass spectroscopy. Started career in Pharma R&amp;D as a scientist with hands on experience on high end instruments like LC/MS, XRD &amp; NMR. Developed &amp; published application notes using Chromatographic techniques on real world samples/issues at various levels.</blockquote>

Agilent Technologies: Ask The Expert - Peptide Workflow

Ask The Expert - Peptide Workflow

Join us to unlock full potential of your workflows, enhance your technical skills

As global awareness of PFAS contamination grows, regulatory scrutiny continues to intensify. In this session, Dr. Rainer Lohmann—Director of the University of Rhode Island’s STEEP Superfund Research Center—will examine how passive sampling strategies can support robust PFAS monitoring in complex environmental matrices. Drawing from real-world studies, Lohmann will explain how these tools help overcome persistent challenges in detecting and quantifying PFAS across air and water systems, and what scientists need to know to stay ahead of evolving regulatory demands.Analyzing PFAS in complex environmental matrices can often impact laboratories with time-consuming sample preparation and contaminated LC/MS/MS systems. The PerkinElmer QSight 500 LC/MS/MS System allows for minimized sample preparation and system contamination thanks to its StayClean Technology, offering unmatched robustness, even with complex matrices.By adding the use of dedicated PTFE-free consumables kits and EPA-compliant software reporting features, the QSight 500 LC/MS/MS System helps labs streamline PFAS workflows. Join this presentation for real-life examples and much more.<h5>By attending this presentation, you will:</h5><ul><li>Discover key regulatory developments shaping PFAS monitoring requirements.</li><li>Explore passive sampling techniques for PFAS detection in air and water.</li><li>See real-world examples illustrating challenges and solutions for testing diverse environmental matrices.</li><li>Understand the challenges of analyzing PFAS in heavily contaminated environmental samples such as soil, sludge, and wastewater and their impact on lab efficiency and instrument performance.</li><li>Discover how the QSight® 500 LC/MS/MS System’s StayClean™ Technology minimizes system contamination and maintenance, ensuring reliable PFAS analysis in even the dirtiest matrices.</li><li>Learn how to enhance PFAS workflow efficiency through the use of PTFE-free consumables and EPA-compliant software, reducing prep time and ensuring accurate, streamlined reporting.</li></ul><blockquote>Presenter: Dr. Rainer Lohmann (Professor, University of Rhode Island’s Graduate School of Oceanography)Dr. Rainer Lohmann is a Professor at the University of Rhode Island’s Graduate School of Oceanography. He obtained a degree in Chemical Engineering and a Doctorate in Environmental Science. He is Director of the URI-led Superfund Research Program Center on the Sources, Transport, Exposure and Effects of PFAS (STEEP). His research focuses on the detection, bioaccumulation, transport, and fate of anthropogenic pollutants in the environment, often relying on passive samplers in the process. Since 2000, he has published &gt; 200 publications and book chapters.Presenter:&nbsp;Tom Hey (Global Environmental Market Leader, PerkinElmer)Tom is Global Market Leader for the environmental segment at PerkinElmer, leveraging his sales and management experience from Key Account Manager and Business Leader positions since joining in 2015. Holding a Ph.D. in Inorganic Chemistry from the University of Bristol, his problem-solving skills are leveraged when figuring out environmental solutions. His passion lies in enhancing PerkinElmer's offerings, particularly in tackling environmental challenges like PFAS and microplastics.</blockquote>

Separation Science: Experience Maximized Productivity for PFAS Analysis, Even with Complex Matrices

Experience Maximized Productivity for PFAS Analysis, Even with Complex Matrices

Learn how to overcome persistent challenges in detecting and quantifying PFAS with the LC/MS/MS

LCMS webinars focusing on LC/MS/MS - page 26

Analysis of Glucagon-Like-Peptide-1 (GLP-1) Analogues

Experience Maximized Productivity for PFAS Analysis, Even with Complex Matrices

Preparing for next generation LC-MS based proteomics

Alternative Fragmentation Modes – EAD, CID and more

ASO RNA impurity analysis

Advanced IP-RPLC-MS Strategies for High-Resolution Oligonucleotide Impurity Profiling

Advantages of HRMS for Quantitative Workflows

Ask The Expert - Peptide Workflow

Oligonucleotides

State of the Art Oxylipin Analysis and New Developments

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