An international team led by researchers from CEITEC Masaryk University has developed a computational method for designing entirely new antimicrobial peptides – short proteins capable of killing bacteria. Instead of relying on the lengthy process of searching for suitable molecules in nature, the researchers can now use molecular simulations to predict their properties and design new molecules with specific functions. The resulting peptides successfully eliminated bacteria resistant to conventional antibiotics and proved effective in preclinical mouse models. The findings introduce a new approach to developing future antibiotics as well as other biologically active peptides.According to the World Health Organization, antibiotic resistance is one of the greatest global health threats of our time. Every year, the number of bacteria resistant to available antibiotics continues to grow. At the same time, developing new drugs is a lengthy and costly process in which most candidate molecules ultimately fail.Researchers at CEITEC Masaryk University have therefore taken a different approach. Rather than searching randomly for antimicrobial compounds, they developed a method for designing them based on molecular design principles. Using molecular simulations, they analysed around 150 peptides in detail and identified the rules that govern the design of molecules capable of forming stable pores in bacterial membranes. These tiny openings disrupt the membrane barrier, causing bacteria to lose control of their internal environment and ultimately die. "We discovered how to arrange specific amino acids so that the resulting peptides form pores in bacterial membranes. This now allows us to generate an enormous number of peptide candidates and select those with the properties we are looking for," says <a target="_blank" rel="noopener noreferrer" href="https://www.ceitec.eu/prof-robert-vacha-ph-d/u27252">Robert Vácha</a> from CEITEC Masaryk University, who led the research.The researchers validated the most promising peptide designs experimentally. They confirmed their activity against a group of the most dangerous antibiotic-resistant bacteria. The best results were achieved against Acinetobacter baumannii, which the World Health Organization classifies as a priority drug-resistant pathogen. The team also demonstrated that their most successful peptide does not damage human red blood cells and shows no significant toxicity towards human cells. Its efficacy was further confirmed in two preclinical mouse models of bacterial infection.The significance of the study lies not only in identifying a new antibiotic candidate but, more importantly, in establishing a new design strategy. Based on their findings, the researchers developed a set of design principles and 52 sequence templates that can be used to design approximately 10 trillion molecules, providing other research teams with a framework for developing new membrane-disrupting peptides. The same principle that proved successful against bacteria could also be applied in the future to develop anticancer therapeutics, biosensors, or targeted drug delivery systems."Until now, researchers have mostly searched for biologically active molecules created by nature and only then investigated how they work. We reversed this process. First, we studied which molecular properties are required for a particular mechanism of action – in our case, the ability to stabilize membrane pores – and then used this knowledge to design entirely new peptides that make such pores. This approach could significantly accelerate the development of new medicines and help us keep pace with the growing challenge of antibiotic resistance," adds Robert Vácha, who has received ERC grants for his research.The study was carried out in collaboration with researchers from the University of Pennsylvania, the University of Groningen, Palacký University Olomouc, and the Institute of Microbiology of the Czech Academy of Sciences. The results were published in <a target="_blank" rel="noopener noreferrer" href="https://www.nature.com/articles/s41589-026-02269-z.epdf">Nature Chemical Biology</a>.<blockquote><h4>The original article</h4><h4><a target="_blank" rel="noopener noreferrer" href="https://www.nature.com/articles/s41589-026-02269-z#citeas">Computational design of antimicrobial peptide nanopores</a></h4>Rahul Deb, Marcelo D. T. Torres, Ivo Kabelka, Jan Přibyl, Kateřina Dvořáková Bendová, Edo Vreeker, Markéta Koběrská, Gabriela Balíková Novotná, Miloš Petřík, Giovanni Maglia, Cesar de la Fuente-Nunez &amp; Robert VáchaNat. Chem. Biol., 2026, 22, 1–12<a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1038/s41589-026-02269-z">https://doi.org/10.1038/s41589-026-02269-z</a>&nbsp;<h6>Licenced under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/">CC-BY 4.0</a></h6></blockquote><h4>Abstract</h4>Antibiotic resistance is a global health threat, driving the need for new molecules that kill bacteria via nontraditional mechanisms. Here, we present a computational de novo design strategy for α-helical peptides that self-assemble into large, stable and membrane-spanning nanopores with antimicrobial activity, including in vivo efficacy against drug-resistant pathogens. Molecular dynamics simulations guided the selection of sequences for transmembrane barrel-stave pore formation, which were validated by microscopy, electrophysiology and fluorescence assays. Using computational and experimental analyses, including negative design controls, we developed general design guidelines and 52 modular sequence templates with tunable antimicrobial, pore-forming properties. Mechanistic studies confirmed bacterial cytoplasmic membrane disruption via designed nanopore formation. A tuned lead peptide selectively killed drug-resistant ESKAPEE bacteria, including Acinetobacter baumannii, without harming human cells, and showed anti-infective efficacy in preclinical mouse infection models. The framework presented here enables the design of synthetic peptide nanopores for precision antimicrobials, anticancer agents, molecular sensors and delivery systems.

New Antibiotics Designed on a Computer: Scientists Develop a Blueprint for Building Molecules Against Drug-Resistant Bacteria 

A new study published in Nucleic Acids Research identifies short “start–stop” elements as highly effective regulators of protein synthesis in human cells. The study was co-led by Leoš Shivaya Valášek from IMIC CAS.<section><div><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/MBU_Nenapadne_start_stop_brany_reguluji_tvorbu_bilkovin_v_bunce_2_4d91bb348d.jpg" alt="MBU: Unassuming Start–Stop “Gates” Regulate Protein Production in Cells" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_MBU_Nenapadne_start_stop_brany_reguluji_tvorbu_bilkovin_v_bunce_2_4d91bb348d.jpg 245w," sizes="100vw" width="720" height="390"><section><div>An international team of scientists has described a&nbsp;previously overlooked mechanism that regulates the levels of important proteins in human cells. A new study published in Nucleic Acids Research reveals that short regulatory “start–stop“ elements act as highly effective speed-limiting gates of protein synthesis. Compared with previously known regulatory sequences, these elements were found to suppress protein production even more efficiently. At the same time, they help maintain low but stable levels of important proteins in cells, even under stress conditions. The study brought together scientists from the United States, the Czech Republic, Canada, and Sweden. Leoš Shivaya Valášek, Head of the Laboratory of Regulation of Gene Expression at the Institute of Microbiology of the Czech Academy of Sciences (IMIC CAS) was a&nbsp;co-author and one of the corresponding authors of the study.</div></section><section><div>During protein production, ribosomes read and translate information encoded in messenger RNA (mRNA) into amino acids, which are then assembled into a&nbsp;new protein. The researchers focused on an unusual sequence in which a&nbsp;start signal is immediately followed by a&nbsp;stop signal. As a&nbsp;result, the ribosome receives instructions to begin and terminate translation almost simultaneously. Although such an arrangement may appear illogical, it proved to be an important regulatory tool.Start–stop motifs are found in more than 1,400 human genes and are particularly common in genes that control cellular signaling pathways, the stress response, or the activity of transcription factors—that is, proteins that regulate the activity of other genes. These genes must be tightly controlled because even small changes in the amount of their protein products can have significant biological consequences.<h4>Resilience Under Stress</h4>The researchers tested the activity of this regulatory mechanism under stress conditions, including in the ATF4 gene, which plays a&nbsp;key role in the so-called integrated stress response. Cellular stress is typically associated with a&nbsp;global reduction in protein synthesis. The authors demonstrated that regulation mediated by start-stop elements is largely independent of the overall state of translation initiation and therefore remains effective even under cellular stress.<h4>A Stronger Brake Than Known Regulatory Elements</h4>The team compared start–stop sequences with similar regulatory regions known as uTranslons. Although both types of elements suppress protein synthesis, the start–stop sequences proved to be significantly more effective. Ribosomes remain associated with these motives for longer before proceeding to the main coding region of the gene.“Start-stop sequences are specialized regulatory elements that ensure increased ribosome retention, thereby allowing for fine-tuning translation,” says Leoš Valášek from IMIC CAS.The study expands our understanding of how cells fine-tune protein synthesis and may ultimately contribute to research on &nbsp;certain cancer and neurodegenerative disorders, and other diseases linked to disrupted protein production.</div></section><blockquote><h4>The original article</h4><h4><a target="_blank" rel="noopener noreferrer" href="https://academic.oup.com/nar/article/54/13/gkag627/8725953?login=false">Elongationless start–stop elements are stress-resilient translation gates that are more repressive than uTranslons</a></h4>Justin Rendleman, Solomon A Haizel, Shaohuan Wu, Laurelle Lee Young, Junjie Liu, Xinyi Ge, Huijing Zou, Mahabub Pasha Mohammad, Matthew Pressler, Shuvadeep Maity, Vladislava Hronová, Zhaofeng Gao, Anna Hermannová, Anna Smirnova, Amy Lei, Kristina Allgoewer, Daniel Sultanov, Will Edward Hinckley, Ziyue Cheng, Lauren Shelby, Tanubrata Dey, Krzysztof J Szkop, Ivan Topisirovic, Ola Larsson, Maria Hatzoglou, Leoš Shivaya Valášek, Christine VogelNucleic Acids Research (2026), Volume 54, Issue 13&nbsp;<a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1093/nar/gkag627">https://doi.org/10.1093/nar/gkag627</a><h6>licenced under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/">CC-BY 4.0</a></h6></blockquote><h4>Abstract</h4>Start–stop elements are translation regulatory elements in 5′ untranslated regions (UTR) of eukaryotic transcripts, consisting of a start codon immediately followed by a stop codon. In contrast to canonical upstream Translons (uTranslons), they exclude elongation which creates unique properties. We conducted a comprehensive, carefully controlled comparison of human start–stop elements and uTranslons both at a genome-wide level and with targeted reporter assays. We found that start–stops and uTranslons were similar with respect to their presence in the 5′ UTRs of hundreds of genes, in particular transcription factors and signaling molecules, the low transcript levels of the corresponding genes, short RNA half-lives, and the negative effect on downstream translation. However, start–stop containing genes were translationally even more repressed than genes with uTranslons. Analysing the start–stop architecture and diverse ribosome footprinting datasets, we found evidence for a start–stop-specific mechanism that involves repeat cycling between initiation, termination, ribosome splitting, and 60S rejoining—a process possibly modulated by ASCC3 and eIF1. This cycling explained increased ribosome retention at start–stops and was—in contrast to ribosome retention at uTranslons—independent of the global initiation state. Finally, we showed that the start–stop element in human ATF4 augments the core regulatory model by controlling translation of the uTranslons.</div></section>

Unassuming Start–Stop “Gates” Regulate Protein Production in Cells

Why Biologics QC Is So Much Harder Than Small Molecule Pharma

Article

Scientists

Interview

Science and research

The Czech Academy of Sciences (CAS) was established by Act No. 283/1992 Coll. as the Czech successor of the former Czechoslovak Academy of Sciences. It is set up as a complex of 54 public research institutions.

Czech Academy of Sciences

Since its establishment in 2011, CEITEC has quickly developed into a cutting-edge infrastructure for research which performs highly alongside the best institutes in Europe. Among the main priorities of CEITEC are the promotion of a motivating and dynamic international scientific environment, the provision of state-of-the-art research infrastructure, and the policy of open communication and equal opportunities.

CEITEC

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

Organomation

Bruker

Thermo Fisher Scientific

Shimadzu Corporation

SCIEX

Waters Corporation

Measurements of drugs of abuse in blood in a forensic lab require highest reliablity with regard to identification and quantification of the compounds in question. After economical evaluation, the analytical setup of the forensic lab was completely rearranged, now processing up to 8000 blood samples each year including a multiple of different measurements.
Drug screening is no longer based on immunoassays lacking selectivity. It is now performed on LC/MS-Toxtyper systems directly providing quantification of five drugs as key compounds. Analysis of THC and further drugs such as neuroleptics and sedatives is carried out by LC/MS/MS.
Recently, a robotic system for sample preparation has been put into service transforming the laboratory process into a fully scalable application for high-throughput measurements.
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Presenter: Christian Vidal (Chemistry Department, State Criminal Investigation Office of Lower Saxony, Hannover, Germany)
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Pixabay/RenoBeranger: Drugs of abuse in blood - high-throughput measurements in a forensic lab

Drugs of abuse in blood - high-throughput measurements in a forensic lab

The ZenoTOF 7600 system was ranked the most innovative technology by The Analytical Scientist for its ability to help scientists address analytical challenges across many markets. Zeno trap coupled with electron activated dissociation (EAD) fragmentation technology unlocks sensitivity gains allowing you to uncover new information for certainty in your results to make better-informed decisions, faster.
Highlights of this technology:
<ul>
<li>Drive new limits of quantification achievable with accurate mass</li>
<li>Detect up to 20x more ions in every experiment</li>
<li>Deliver high depth of coverage on low abundance species, quickly and robustly with Zeno SWATH data-independent acquisition (DIA)</li>
</ul>
<blockquote>
Presenter: Bhavya Shukla (Sales Development Manager, SCIEX)
</blockquote>
<blockquote>
Bhavya Shukla, Sales Development Manager at SCIEX has more than 8 years of experience in the analytical industry. He pursued his post-graduation in chemical engineering from the Institute of Chemical Technology Mumbai. His major role is to support LCMS users by providing them optimal solutions through a keen understanding of their needs.
</blockquote>

SCIEX: Leveraging the power of Zeno trap and EAD

Leveraging the power of Zeno trap and EAD

Zeno trap coupled with electron activated dissociation (EAD) fragmentation technology unlocks sensitivity gains allowing you to uncover new information

Presentation Topics
<ul>
<li>Origins of the Digital Ion Trap
</li>
<li>Ion Trap v. Digital Ion Trap
</li>
<li>Shimadzu&#39;s Journey to the MALDI Digital Ion Trap
</li>
<li>Basic Proteomics
</li>
<li>Glycomics
</li>
<li>Antibody Drug Conjugates
</li>
<li>Summary and Acknowledgements
</li>
</ul>

Shimadzu: Proteomic Analysis Using a Miniature MALDI Digital Ion Trap Mass Spectrometer

Proteomic Analysis Using a Miniature MALDI Digital Ion Trap Mass Spectrometer

Proteomic Analysis Using a Miniature MALDI Digital Ion Trap

In this webinar you will discover how extractables and leachables (E&amp;L) testing can be streamlined using acquisition modes enhanced by QTRAP technology. If you are new to E&amp;L testing or want to learn how your own workflows can be improved when using nominal mass technology then this webinar is for you.
Key topics that will be covered in this webinar include:
<ul>
<li>Introduction to E&amp;L analysis using nominal mass instrumentation</li>
<li>How the QTRAP can enhance E&amp;L analysis</li>
<li>The importance of libraries and how they can be implemented to improve compound identification</li>
</ul>
<blockquote>
Presenter: Ferran Sanchez (Market Development Manager, Pharma/CRO (MS &amp; CE), EMEAI, SCIEX)
</blockquote>
<blockquote>
Ferran obtained his PhD in Pharmaceutical Sciences at the University of Barcelona in 2005 and has been involved with mass spectrometry ever since. He has worked for SCIEX for 18 years holding different positions in sales, marketing and business development covering the EMEAI region. During this time, Ferran has been working closely with customers in the pharmaceutical industry to deepen his understanding of the market and user needs for delivering the right solutions at the right time.
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<blockquote>
Presenter: Jack Steed, Sr. (Technical Specialist, SCIEX)
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Jack joined SCIEX in 2019 as a technical specialist, his main responsibilities include the creation and proliferation of technical marketing content such as application notes and presentations as well as having a strong focus on the pharma market and small molecule analysis. Prior to joining SCIEX, Jack was employed by a CRO working mainly in small molecule method development and validation, with an emphasis on LC and LC-MS analysis.
</blockquote>

SCIEX: Extractables and leachables: the complete workflow using QTRAP LC-MS/MS technology

Extractables and leachables: the complete workflow using QTRAP LC-MS/MS technology

Discover how extractables and leachables (E&L) testing can be streamlined using acquisition modes enhanced by QTRAP technology.

Extractables and leachables: QTRAP LC-MS/MS workflow

Rebroadcast of the Live from the Lab: Solutions for Multi-Omics Research from June 13, 2024
The new Stellar MS - Instrumentation that scales analytical throughput reliably and practically
How can you bridge the gap between discovery and the clinical research? 
With the new Thermo Scientific Stellar MS, it’s now easier than ever to go from discovery to validation with unrivaled quantitation at scale.
Key learning points
<ul>
<li>Meet the most advanced ion trap platform, the new Stellar MS system with acquisition rates of 100Hz+, MS3, and HCD/Resonance CID.</li>
<li>Hear how PRM Conductor Software helps bridge discovery to targeted gap, eliminates/reduces scripting+Microsoft® Excel, and automates refinement/method creation.</li>
<li>Learn how intelligent acquisition provides adaptive RT for higher throughput and robust operation, and dynamic AGC for best quantitation.</li>
</ul>
Can&#39;t attend the rebroadcast? No problem! Register anyway and you will automatically receive the link to the recording. 
<blockquote>
Presenter: Hamish Stewart (Senior Staff Scientist, Thermo Fisher Scientific)
</blockquote>
<blockquote>
Hamish Stewart is a Senior Staff Scientist at Thermo Fisher Scientific Bremen. He is the lead scientist for the Orbitrap Astral and a developer of Orbitrap instrumentation, responsible for research on future commercial mass spectrometers, novel related concepts and technologies.
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Previously, he obtained his PhD in Physical Chemistry from the University of Nottingham and then worked for Shimadzu Research Laboratory (Europe) Ltd.
</blockquote>
<blockquote>
He is the holder of 65 patents and is the winner of The George N Hatsopoulos Technical Innovation Award.
</blockquote>

The new Stellar MS - Instrumentation that scales analytical throughput reliably and practically

With the new Thermo Scientific Stellar MS, it’s now easier than ever to go from discovery to validation with unrivaled quantitation at scale.

The new Thermo Scientific Stellar MS

Join us to explore the versatile power of the QTRAP LC-MS/MS system in food analysis and contaminant detection, including phytochemical profiling, targeted/untargeted analysis, trace contaminant detection, food authenticity, and nutraceutical development.<h5>Key highlights:</h5><ul><li>QTRAP LC-MS/MS system in enabling comprehensive phytochemical analysis in food and fruits</li><li>Validated sMRM quantitation of essential health-promoting phytomarkers</li><li>Untargeted and targeted procedures to define the extensive phytochemistry of food</li><li>Capability to identify contaminants such as pesticid and, drug contaminants at trace levels</li></ul><blockquote>Presenter: Dr. Pratibha Srivastava (Agharkar Research Institute)</blockquote>

SCIEX: QTRAP LC-MS/MS system: a versatile platform for food analysis and contaminant detection

QTRAP LC-MS/MS system: a versatile platform for food analysis and contaminant detection

Join us to explore the versatile power of the QTRAP LC-MS/MS system in food analysis and contaminant detection.

QTRAP LC-MS/MS for food analysis and contaminant detection

<div>The Waters Xevo CDMS delivers game-changing improvements in the measurement and characterization of high mass and highly heterogeneous compounds, paving the way for breakthroughs in fields such as gene therapy and structural biophysics.Join us for this webinar to explore how the Waters Xevo CDMS is revolutionizing the analysis of complex biomolecules.Learn how cutting-edge innovations are transforming research-grade technology into accessible, high-performance tools - enabling simplified, compliant workflows and deeper insights into rAAVs, VLPs, mRNA/LNPs, and more.<ul><li>Gain insights on Waters Xevo CDMS product, from the nanoESI emitter, to ELIT. Learn the development journey of the research grade CDMS technology from Indiana University into a commercial product that enables the democratization of the novel technology.</li><li>Learn application space of the Waters Xevo CDMS, hearing application examples based on collaboration with Key Opinion Leaders from the Pharma and Biotech industry and from various research institutes.</li><li>Hear from Pfizer scientist to examine how ELIT CDMS has evolved through commercialization, address key considerations for introducing Xevo CDMS into an industrial setting and highlight user experiences across multiple modalities with Xevo CDMS.</li></ul><blockquote>Presenter: Lauren Barnes, Ph.D. (Senior Scientist, Pfizer)Dr. Lauren Barnes is a Senior Scientist at Pfizer within the Biotherapeutics and Pharmaceutical Sciences division at Pfizer. She joined Pfizer September 2022 as a mass spectrometrist within the Analytical Research &amp; Development (ARD) organization performing heightened characterization on biotherapeutic molecules, including proteins and gene therapies. In this role, she has expanded her expertise to include mass photometry, leveraging her background in the analysis of large, intact biomolecular species to develop methods for species characterization with this emerging technique. Lauren has contributed to collaborative efforts involving CDMS, both during her graduate research and in her professional role at Pfizer.Lauren received her Ph.D. in Analytical Chemistry from Indiana University Bloomington in 2022. Her graduate research focused on the analysis of intact viral gene therapy systems using charge detection mass spectrometry (CDMS) in the lab of Dr. Martin Jarrold.Presenter: Jakub Ujma, Ph.D. (Principal Consulting Technical Product Lead, Waters Corporation)Jakub works at Waters Corporation as a Principal Consulting Technical Product Lead in mass spectrometry R&amp;D. His work has focused on Charge Detection Mass Spectrometry (CDMS), with applications in the analysis of large biomolecules such as protein complexes and virus particles. Jakub leads the development of the Waters Xevo™ CDMS system, which utilizes an electrostatic linear ion trap to enable unambiguous mass measurement of megadalton-sized molecules. In addition to CDMS, Jakub also contributed to a number of projects involving ion mobility and time-of-flight (ToF) mass spectrometry, such as hardware design and performance characterization. He has co-authored several research papers and regularly participates in scientific meetings and discussions within the mass spectrometry community.Jakub received his PhD in Chemistry from Manchester University with a focus on ion mobility techniques for studying protein structure.Presenter: Anisha Haris, Ph.D. (Senior Applications Scientist, Waters Corporation)Anisha is a Senior Applications Scientist in the Charge Detection Mass Spectrometry (CDMS) Program at Waters Corporation. Her work focuses on supporting the evaluation, development, and commercialization of charge detection mass spectrometry (CDMS) for the precise characterization of large, complex, and heterogeneous biomolecules - including protein complexes, virus-like particles, and viral vectors. By bridging cutting-edge instrumentation with real-world applications, Anisha supports the expansion of CDMS through close collaboration with researchers and industry partners in biopharmaceutical development, structural biology, and virology.Anisha received her Ph.D. from the University of Warwick. Her dissertation was focused on “Advanced Applications of Mass Spectrometry for Isomer Differentiation and Analysis of Biomolecules”.</blockquote></div>

Waters Corporation: Unveiling the Waters Xevo CDMS: Biomolecule Characterization Redefined

Unveiling the Waters Xevo CDMS: Biomolecule Characterization Redefined

Join us for this webinar to explore how the Waters Xevo CDMS is revolutionizing the analysis of complex biomolecules.

Waters Xevo CDMS Biomolecule Characterization

Immunoassays dominate the drug screen assay market as the most widely used method for routine urine toxicology screens. However, this method of analysis lacks specificity and suffers from cross-reactivity with irrelevant, similarly structured compounds. Furthermore, not all immunoassays are sensitive to drug metabolites, leading to false negatives. These limitations lead to the need for confirmation testing by LC-MS/MS, which has longer turnaround times. The Toxtyper is an automated LC-MSn coupled with a method-specific library search engine and compound identification algorithm. Its push-button interface is designed for implementation in the lab without the need for toxicology trained staff.
This webinar will be focused on the Toxtyper drugs-of-abuse (DOA) LC-MSn method and how it compares with the currently used immunoassays (CEDIA, EMIT and DRI) for urine toxicology routine panels in terms of sensitivity, number of compounds identified, speed, and sample preparation. The comparative study conducted by Dr. Adina Badea, PhD, DABCC, demonstrated that the Toxtyper provides consistent results with commonly used immunoassay screens, within a competitive timeframe. Furthermore, the added information and specificity provided by the LC-MSn system can have a significant impact in optimization of patient care.
<h3>Key Learning Objectives:</h3>
<ul>
<li>Comparison between the Toxtyper LC-MS and conventional immunoassays</li>
<li>Avantages of using the Toxtyper system to optimize patient care</li>
<li>Using the Toxtyper to elucidate unusual exposures in the emergency medicine setting</li>
</ul>
<h3>Who Should Attend:</h3>
<ul>
<li>Toxicologists</li>
<li>Medical Examiners</li>
<li>Toxicology Lab Supervisors</li>
</ul>
For Research Use Only. Not for use in clinical diagnostic procedures.
<blockquote>
Presenter: Adina Badea (Director of Toxicology at Lifespan / Rhode Island Hospital)
</blockquote>
<blockquote>
Dr. Adina Badea, PhD, DABCC, received her clinical chemistry and toxicology training from UCSF, where she worked under the supervision of Dr. Alan Wu and Dr. Kara Lynch on developing methods and finding new solutions to current challenges in clinical toxicology testing. Currently she is Director of Toxicology at Rhode Island Hospital and Assistant Professor of Pathology and Laboratory Medicine at The Warren Alpert Medical School of Brown University, where she focuses on expanding the capabilities of the clinical toxicology lab using high resolution mass spectrometry and investigating emerging matrices.
</blockquote>

Bruker Daltonics: Moving Away From Immunoassays: Adapting LC-MS for Routine Urine Toxicology Screens

Moving Away From Immunoassays: Adapting LC-MS for Routine Urine Toxicology Screens

<h4>Join us to see how CDMS extends the reach of mass spectrometry - turning molecular complexity into actionable insight.</h4>As biomolecular systems grow larger and more heterogeneous, conventional MS reaches its limits. Charge detection mass spectrometry (CDMS) overcomes these challenges by directly measuring the mass of individual ions. In this webinar, two experts show how CDMS enables accurate characterization of complex systems in biopharma and structural virology. Dr. Andi Flütsch (Johnson &amp; Johnson) examines heterogeneous glycoprotein vaccines, while Prof. Charlotte Uetrecht (University of Lübeck, CSSB) reveals viral capsid heterogeneity and assembly using norovirus.<h4>Why you should attend</h4><ul><li>Understand why CDMS matters for analyzing highly heterogeneous, high mass biomolecules beyond the limits of conventional native MS.</li><li>See how CDMS solves real biopharma challenges, enabling characterization and comparability of complex glycoprotein vaccines where traditional analytics fall short.</li><li>Gain new insight into viral heterogeneity, learning how CDMS reveals mass, stoichiometry, and assembly features inaccessible with native MS alone.</li></ul><h4>Who should attend</h4><ul><li>Scientists and engineers working with complex molecular or particulate systems across chemistry, biology, biopharma, materials, and nanoscience</li><li>Analytical and structural science leaders looking to push beyond the limits of conventional mass spectrometry for heterogeneous, high mass samples</li><li>R&amp;D managers and decision makers evaluating next generation analytical technologies to enable deeper insight and more confident decisions</li></ul><blockquote>Speaker: Charlotte Uetrecht (Professor/Scientific Director, University of Lübeck/Centre for Structural System Biology (CSSB))Professor Charlotte Uetrecht has been Full Professor of Chemistry at the University of Lübeck since 2024, co director of the Institute of Chemistry and Metabolomics, and Scientific Director of the Centre for Structural Systems Biology (CSSB) since 2026. She leads the Dynamics of Viral Structures group, focusing on large viral protein complexes using native mass spectrometry and complementary structural methods, with emphasis on coronaviruses and norovirus particles. She earned her Ph.D. from Utrecht University under Prof. Albert J.R. Heck.Speaker:&nbsp;Andi Flütsch (Associate Director, Analytical &amp; Process Development, Johnson &amp; Johnson Innovative Medicine)Dr. Flütsch is an Associate Director in Analytical &amp; Process Development at Johnson &amp; Johnson Innovative Medicine based in Switzerland. He has extensive experience in analytical development and protein characterization, supporting products from late-stage development through commercialization. His work focuses on advanced analytical technologies and GMP‑ready analytical strategies for complex modalities such as glycoproteins and viral vectors. Dr. Flütsch received Ph.D. from University of Zurich in 2013 in Biochemistry and Molecular Biology.</blockquote>

Waters Corporation: CDMS Applied: Bridging Molecular Complexity and Clarity from Bioconjugates to Viruses

CDMS Applied: Bridging Molecular Complexity and Clarity from Bioconjugates to Viruses

CDMS enables analysis of complex biomolecules beyond native MS. Discover applications in glycoprotein vaccines and viral structure characterization.

LCMS webinars focusing on LC/IT - page 1