<p><strong>Professor Michaela Rumlová, head of a research group of the National Institute of Virology and Bacteriology at UCT Prague (and Vice-Rector for doctoral studies), holder of a licensed patent &nbsp;for antiretroviral testing assays, and recipient of the Czech Science Foundation’s President’s Award for HIV research, has also become the principal investigator of the bilateral INTER-EXCELLENCE II project “</strong><i><strong>Cellular factors regulating the export and packaging of unspliced ​​retroviral RNA</strong></i><strong>”, starting this year. In this interview, she explains how retroviruses such as HIV “hack” the cell in order to export their own genome from the nucleus into the cytoplasm, and then to the site where it is specifically packaged into nascent viral particles, a key step in viral replication. Her team is collaborating with the NIH (National Institutes of Health) and Rockefeller University to elucidate mechanisms that may help reveal new vulnerable points in the retrovirus replication cycle while simultaneously clarifying related cellular processes.</strong></p><h5><strong>Could you describe your project and its main objectives?</strong></h5><p>Retroviruses, such as HIV, are viruses that carry genetic information in the form of RNA; however, after entering a cell, they are able to reverse transcribe it into DNA and integrate it into the host genome. In order to replicate, they must transport their genetic information—in the form of unspliced RNA—from the nucleus into the cytosol. There, it serves both as a template for the production of viral proteins and as the genome of new viral particles. This is highly unusual, as the cell very carefully controls which RNA molecules are allowed to leave the nucleus. Normal protein-coding cellular RNAs, known as messenger RNAs (mRNAs), must undergo splicing—a processing step in which certain segments are removed—before being exported. When this process fails, mRNA that retains these segments is held back in the nucleus as part of quality control and subsequently degraded. Retroviruses have managed to outwit this cellular control machinery, allowing their unspliced RNA to pass into the cytoplasm.</p><p>Our project focuses on identifying the cellular proteins that assist retroviruses in this step and on the mechanism by which protein complexes bound to viral RNA are remodelled during RNA transport. The goal is to understand how the virus uses cellular mechanisms to its advantage and how this pathway is linked to the subsequent fate of the RNA, i.e. to its translation and packaging into new viral particles.</p><h5><strong>Why is this export of unspliced ​​RNA so important for retroviral replication?</strong></h5><p>Because this RNA has a dual role for the virus. On the one hand, it serves as a template for synthesizing viral proteins in the cytoplasm; on the other, it represents the genetic material itself, which must be packaged into new viral particles. The virus must package its RNA genome in its unspliced form, as only this RNA contains essential sequences without which further viral replication would be impossible.</p><p><strong>Simply put: </strong>the virus needs to get a complete copy of its genetic instructions out of the nucleus. Once the viral RNA is in the cytoplasm, it can be used as a template for synthesizing viral proteins; and a portion of these RNA molecules is then selected and packaged into a new particle as a genome. We are interested in how the virus forces the cell to allow viral RNA that is, from the cell’s perspective, “unfinished,” that is unspliced, to leave the nucleus. We are also investigating how the cell and the virus together - albeit unintentionally from the cell’s perspective - determine which RNA molecule will be translated into proteins and which will be packaged as the genome. This is one of the key, yet still not fully understood, steps of retroviral replication.</p><h5><strong>What do you think it was about your project that impressed the Ministry of Education, Youth and Sports’ jury the most?</strong></h5><p>I believe the decisive factor was a combination of several elements. First, the reviewers were primarily interested in the scientific problem itself. We are investigating a mechanism that is essential for retroviruses, but still not sufficiently understood, which may also have broader implications for the regulation of cellular processes. In addition, the quality of the team, our strong collaboration with the<strong> NIH </strong>and <strong>Rockefeller University</strong>, and the use of modern methods that will allow us to track viral RNA in great detail also played a role. It was also important that the project has clear objectives and a realistic plan.</p><h5><strong>How will this research contribute to the development of new treatments for retroviral infections?</strong></h5><p>It is important to say that this is primarily basic research. Rather than developing a new drug directly, we are trying to understand, at the molecular level, the step that the virus cannot do without. Only when we fully understand the mechanism of these cellular processes and identify the essential factors for the export of unspliced ​​RNA and how they function, will we be able to better determine which interactions or mechanisms represent potentially vulnerable points. Similar mechanisms associated with the export of unspliced ​​mRNA also appear in some diseases, such as cancer, so I &nbsp;see the benefit of our research mainly in that it will refine our understanding of these pathological processes in the cell, and retroviruses help us do so. Therefore, our work on retroviruses not only shows us how the virus works, but also how the cell itself works.</p><h5><strong>What responsibilities does your UCT Prague team have? How does the collaboration with your American partners work?</strong></h5><p>At UCT Prague, we are conducting the project’s primary experimental work. Our research involves cell cultures, viral models, and various biochemical techniques ranging from immunochemistry to microscopy that allow us to track viral RNA and identify its cellular partners. In collaboration with colleagues from <strong>NIH, Frederick</strong>, we are developing single-particle tracking methods to observe viral RNA movement in living cells across both space and time. Furthermore, we are working with colleagues from <strong>Rockefeller University to employ iCLIP </strong>methods for the precise mapping of protein-binding sites on RNA. Both collaborations are valuable to us, because they are not just about data sharing, but also about the transfer of expertise and detailed know-how.</p><h5><strong>Who else is collaborating on the project?</strong></h5><p>At UCT Prague, we collaborate closely with the Department of Biotechnology and the Department of Biochemistry and Microbiology. Externally, we work with colleagues from the Institute of<strong> Organic Chemistry and Biochemistry of the CAS (IOCB Prague)</strong> and the <strong>Central European Institute of Technology in Brno (CEITEC)</strong>. Our research naturally necessitates the integration of diverse fields of expertise; it requires combining virology, cell biology, and biochemistry with advanced imaging and modern approaches to study RNA-protein interactions. This is exactly what makes our project capable of addressing complex questions that a single laboratory cannot tackle on its own.</p><h5><strong>Are there plans to continue the project? Have you brought on new collaborators, and are you looking to welcome new colleagues to the team?</strong></h5><p>Yes, definitely. In basic research, it often happens that one answered question opens up several more. High-quality, properly interpreted data provide a foundation you can build on — and that is what moves scientists forward. It is already clear that the topic of retroviral RNA export and packaging has broader implications and may reveal more general principles of how RNA functions within the cell. We also hope the project will be attractive to students, as it connects classical molecular biology, biochemistry, and virology with cutting-edge biotechnological methods. Students are already involved in the project as part of their bachelor’s and master’s theses.</p><h5><strong>What was the personal turning point that motivated you to pursue a long-term investigation into retroviral particles?</strong></h5><p>I first encountered retroviruses in the early 1990s during my diploma thesis, when I was working at IOCB Prague on HIV-1 protease inhibitors. At that time, AIDS could not yet be effectively treated, and retrovirus research had a completely different dimension. From the very beginning, I was fascinated by how such a relatively small and simple virus can outsmart evolutionarily highly optimized cellular processes and turn them to its own advantage. And that has never stopped fascinating me. From a scientific point of view, retroviruses are remarkable; just consider one of their enzymes, reverse transcriptase, without which no diagnostic or research laboratory in the world could function today. Without it, it would be impossible to diagnose RNA viruses like SARS-CoV-2, influenza, or HIV using RT-PCR tests, or, for example to produce recombinant human proteins in bacterial cells.</p>

Tracking unspliced RNA: Professor Rumlová studies how retroviruses “hack” cells

News from LabRulezLCMS Library - Week 20, 2026

<p><strong>🎤Lindsay Repka&nbsp;</strong></p><p><strong>Lindsay Repka is a chemistry professor at Middlebury College whose research explores photoredox chemistry, catalyst stability, and visible-light-driven transformations. Her lab emphasizes both mechanistic insight and hands-on student training in advanced analytical instrumentation.</strong></p><p>In this episode of Concentrating on Chromatography, we sit down with Lindsay Repka to discuss how LC-MS and GC-MS transformed her lab’s approach to photoredox chemistry.</p><p>What began as a project to develop a visible-light photocrosslinking handle unexpectedly led to a major discovery: the solvent (DMF) was reacting with the photocatalyst itself. Using high-resolution LC-MS, Lindsay’s team observed multiple solvent adducts forming — sometimes with complete catalyst consumption. That discovery reshaped their research direction.</p><p>This episode is a rare deep dive into both LC-MS and GC-MS within the same research project, showing how chromatography-driven insight can turn unexpected degradation into productive new reactivity.</p><p><strong>If you work in:</strong></p><ul><li>Photoredox chemistry</li><li>Reaction optimization</li><li>Mass spectrometry method development</li><li>Catalyst screening</li><li>Academic synthetic chemistry</li></ul><p>…this conversation will resonate.</p><h4><strong>Key Topics Covered</strong></h4><ul><li>Photocatalyst stability in DMF, DCE, and MeCN</li><li>Demethylation under mild visible-light conditions</li><li>High-resolution Q-TOF LC-MS quantitation</li><li>Internal standard methodology in GC-MS</li><li>Signal-to-noise improvement using extracted ion chromatograms</li><li>Reaction reproducibility and quality control strategy</li></ul><h3><strong>Video Transcription</strong></h3><p>In this interview, Lindsay Repka discusses the role of photoredox chemistry in method development, photocrosslinking, solvent activation, catalyst stability, and the use of LC-MS and GC-MS to understand reaction pathways.</p><h4><strong>What is photoredox chemistry?</strong></h4><p>Photoredox chemistry uses light to activate a photocatalyst, which can either donate or accept an electron from a substrate. This generates radical species that can undergo new types of reactivity.</p><p>Repka explains that one of the key advantages of photoredox chemistry is its ability to operate under mild conditions, often using visible light. This makes it attractive for sensitive molecules and biological systems, including potential applications in drug release, live-cell chemistry, and drug development.</p><h4><strong>Photocrosslinking and drug-target interactions</strong></h4><p>Repka’s group initially aimed to develop visible-light photocrosslinking methods to study drug interactions with biological targets. Photocrosslinking can covalently link a drug to its target, making it easier to identify the biological target of a compound.</p><p>Traditional photocrosslinking often uses UV light, but visible light offers milder and more biologically compatible conditions.</p><h4><strong>From photocrosslinking to solvent activation</strong></h4><p>The project shifted direction when the desired photocrosslinking reactions gave very low yields. Instead of reacting with amino acids as intended, the radical intermediate mainly reacted with itself.</p><p>The team explored different solvents to stabilize the radical, but found that some solvents, such as DMF, were not inert. Instead, the solvent reacted with the photocatalyst or radical species, revealing unexpected solvent activation chemistry.</p><h4><strong>Why LC-MS was critical</strong></h4><p>LC-MS became essential because the reaction mixtures were too complex and low-yielding for NMR or GC-MS. High-resolution LC-MS allowed the team to detect minor products, identify photocatalyst modifications, and observe solvent addition products with high confidence.</p><p>Repka emphasizes that LC-MS was both a qualitative and quantitative tool. It was used quantitatively to measure how much photocatalyst remained after light exposure, and qualitatively to identify degradation products and new reactivity pathways.</p><h4><strong>Photocatalyst stability workflow</strong></h4><p>The team developed a systematic workflow to evaluate photocatalyst stability under light exposure. Because catalyst degradation was time-sensitive, reproducibility required strict control of experimental conditions.</p><p>Key steps included using a glove box, commercial deoxygenated solvents, accurate weighing on a microbalance, controlled light exposure in a photoreactor, and temperature control with a chiller. These precautions helped reduce day-to-day variability and enabled reproducible measurements of catalyst remaining.</p><h4><strong>Quantifying catalyst remaining by LC-MS</strong></h4><p>Calibration curves were prepared using pure photocatalyst solutions and LC-MS ion areas. The team worked in the nanomolar range to maintain linearity.</p><p>Instead of relying only on total ion chromatograms, they used extracted ion chromatograms (EICs) to improve signal-to-noise for the photocatalyst signal. Baseline subtraction was also applied to reduce noise and improve quantitation at low concentrations.</p><p>Calibration curves and quality control samples were prepared and measured on the same day as the reaction samples, because LC-MS signal intensity can vary significantly from day to day.</p><h4><strong>Why GC-MS was used later</strong></h4><p>For demethylation studies, the group moved to GC-MS because the substrates and products were small and volatile enough for gas chromatography. GC-MS was better suited for rapidly screening many reaction conditions, including different photocatalysts, solvents, and oxidants.</p><p>Instead of generating full calibration curves for every experiment, the team used an internal standard to streamline analysis and determine percent conversion based on relative response factors.</p><h4><strong>Practical lessons from the project</strong></h4><p>Repka highlights the importance of careful sample preparation, especially when working with very small quantities of photocatalysts. A high-quality microbalance, stable granite platform, antistatic tools, and aluminum weigh boats improved weighing accuracy and reproducibility.</p><p>She also argues that mass spectrometry should be a standard part of photoredox method development because it can reveal minor products, support reaction optimization, and provide insights that may be difficult or impossible to obtain by NMR alone.</p><h4><strong>Final perspective</strong></h4><p>Beyond the chemistry, Repka emphasizes the importance of student training and mentoring. For her, research is not only about discovering new reactivity but also about giving students practical experience, helping them develop independence, and preparing them for future scientific careers.</p><blockquote><p><strong>This text has been automatically transcribed from a video presentation using AI technology. It may contain inaccuracies and is not guaranteed to be 100% correct.</strong></p></blockquote><blockquote><h4><strong>Concentrating on Chromatography Podcast</strong></h4><p>Dive into the frontiers of chromatography, mass spectrometry, and sample preparation with host David Oliva. Each episode features candid conversations with leading researchers, industry innovators, and passionate scientists who are shaping the future of analytical chemistry. From decoding PFAS detection challenges to exploring the latest in AI-assisted liquid chromatography, this show uncovers practical workflows, sustainability breakthroughs, and the real-world impact of separation science. Whether you’re a chromatographer, lab professional, or researcher you'll discover inspiring content!</p><p>You can find <strong>Concentrating on Chromatography Podcast </strong>in podcast apps:</p><ul><li><a target="_blank" rel="noopener noreferrer" href="https://open.spotify.com/show/1wZg67rCjoGju4yhqxI3tL"><strong>Spotify</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podcasts.apple.com/tz/podcast/concentrating-on-chromatography/id1788429185"><strong>Apple podcast</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podscan.fm/podcasts/concentrating-on-chromatography"><strong>podscan</strong></a></li></ul><p>and on <a target="_blank" rel="noopener noreferrer" href="https://www.youtube.com/@ChromatographyTalk/videos"><strong>YouTube channel</strong></a></p></blockquote>

Using LC-MS & GC-MS to Decode Photoredox Catalyst Stability

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

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Evosep Biosystems

<p><strong>Unlock new perspectives with our accurate mass 101 webinar series.</strong></p>
<p>Accelerate your workflows and expand your knowledge around accurate mass with these informative webinars.</p>
<p>In this webinar series, SCIEX applications scientists will explain the benefits of using accurate mass, sample analysis, instrument operation and data processing in real-time.</p>
<p>Get the inside scoop and register today!</p>
<h3><strong>Accurate mass 101: non-targeted analysis</strong></h3>
<p>Join us for this webinar to see how to discover the unknown using non-targeted analysis. We will showcase workflows and strategies to drive success with suspect screening and non-target identification. Discover the ability to identify peaks of interest and confidently identify unknown compounds.</p>


SCIEX: Accurate mass 101: non-targeted analysis

Accurate mass 101: non-targeted analysis

SCIEX applications scientists will explain the benefits of using accurate mass, sample analysis, instrument operation and data processing in real-time.

<p><strong>Unleash the power of DIA and enable the exploration of complex biological systems with unprecedented depth and precision for large-scale quantitative protein analysis combined with short methods on the Evosep One.</strong></p>
<h3><strong>Global proteomics with Evosep and DIA-PASEF</strong></h3>
<p>Recent progress in liquid chromatography and mass spectrometry, as well as sample preparation and search algorithms for spectra deconvolution and identification, plays an important role in bringing proteomics to the forefront of drug discovery and development. Nanoflow liquid chromatography coupled to tandem mass spectrometry is one of the most essential elements in a proteomics workflow. The four dimensional ion detection achieved with the latest generation of Bruker’s trapped ion mobility spectrometers led to superior speed and sensitivity. Evosep One liquid chromatography platform offers speed and robustness while maintaining, even exceeding previously achieved performance level with high-performing nano LC systems. We share here some results only possible with this combination of LC-MS and dia-PASEF.</p>
<blockquote>
<p><strong>Presenter:</strong> Anh Reynolds (Scientist, Bristol Myers Squibb)</p>
</blockquote>
<h3><strong>Extending sensitivity limits with Evosep and Slice-PASEF</strong></h3>
<p>Sensitivity improvements in LC-MS proteomics have recently led to exciting new applications, such as comprehensive proteomic profiling of single cells or 2-dimensional proteomics of tissue slices. In this talk, I will describe Slice-PASEF, a new acquisition technology for timsTOF instruments, which, in combination with the DIA-NN data analysis software, provides a fold-change signal boost. When paired with the Evosep system, Slice-PASEF allows to achieve high sensitivity in robust high-throughput workflows, paving a way for accessible sensitive proteomics on a large scale.</p>
<blockquote>
<p><strong>Presenter:</strong> Vladim Demichev (Group Leader, Quantitative ProteomicS, Charité – Universitätsmedizin Berlin)</p>
</blockquote>


Pixabay/sethink: Revolutionizing proteomics with Evosep-DIA

Revolutionizing proteomics with Evosep-DIA

Global proteomics with Evosep and DIA-PASEF & Extending sensitivity limits with Evosep and Slice-PASEF.

<p>Dear user and other PaSER interested customers,</p>
<p>You are hereby invited to our 2nd Virtual PaSER Workshop. A lot of new possibilities has been introduced since last time – including, but not limited to PaSER Novor for de novo sequencing of dda-PASEF® data on the PaSER Box as well as TIMS DIA-NN 2.0 -which will be demonstrated during this Workshop. Data virtualization has been a requested feature – and this is now possible with Mass Dynamics for PaSER. Not limited to above – stay tuned for even more approaching features, we will discuss as well.</p>
<h3><strong>The tentative agenda looks like this:</strong></h3>
<h5><strong>1:00 – 1:15 pm:  Introduction</strong></h5>
<ul>
<li>Willy Bjørklund</li>
</ul>
<h5><strong>1:15 – 1: 35pm:  New Applications on the timsTOF Platform</strong></h5>
<ul>
<li>Lars Kristensen (Field Application Specialist)</li>
</ul>
<h5><strong>1:35 – 1:55 pm:  PaSER as a bioinformatic platform - what’s new and what’s coming</strong></h5>
<ul>
<li>Jonathan Krieger (Software R&amp;D Department)</li>
</ul>
<h5><strong>5 minute break</strong></h5>
<h5><strong>2:00 – 2:20 pm: Live Demo/workshop of PaSER</strong></h5>
<ul>
<li>Tharan Srikumar (Software R&amp;D Department)</li>
</ul>
<h5><strong>2:20 – 2:50 pm: Mass Dynamics</strong></h5>
<ul>
<li>Mark Condina and Giuseppe Infusini</li>
</ul>
<h5><strong>2:50 – 3:10 pm: Questions and discussions</strong></h5>
<h5><strong>3:10 – 3:15 pm:  Conclusion</strong></h5>
<ul>
<li>Willy Bjørklund</li>
</ul>
<p>We aim for a lively interaction so take the timing as an indication. Please feel free to share with colleagues or others you think could benefit from attending this workshop. Looking forward to “meet”</p>


Bruker Virtual PaSER Workshop

Dear user and other PaSER interested customers, You are hereby invited to our 2nd Virtual PaSER Workshop. 

<p><strong>This webinar will focus on untargeted LC/MS Omics solutions that will provide the biological insights needed to produce meaningful results. An emphasis will be spent on an End-to-End HILIC metabolomics workflow for our LC/Q-TOF platform.</strong></p>
<p>This includes automate sample preparation for cells and plasma, a Bio LC that is fit for purpose for metal sensitive analysis, robust and transferable HILIC chromatography, the 6546 LC/Q-TOF data independent analysis of samples, with an ID workflow that includes a new HILIC PCDL with 500 core metabolism analytes with spectra and retention time annotation.</p>
<p>For unknowns not found in Agilent PCDLs, SIRIUS/CSI:FingerID which uses AI predict structure from spectra and conducts online identification search will be demonstrated. A complementary targeted multi-omics workflow will be briefly mentioned before sharing the new Ion Mobility and ExD technologies for high end LC/MS Omics investigations.</p>
<blockquote>
<p><strong>Presenter:</strong> Karen E. Yannell (Omics Workflow Specialist, Agilent Technologies)</p>
</blockquote>
<blockquote>
<p>Karen E. Yannell is an Omics Workflow Specialist at Agilent Technologies. She is an expert in small molecule high throughput analysis by triple quadrupole (TQ) and quadrupole time-of-flight (Q-TOF) mass spectrometry for applied markets. Her recent work has focused on developing targeted metabolomics methods and routine Q-TOF workflows for both expert and non-expert users alike. Previously, Karen worked on forensic, metabolomics, and biomarker discovery applications with ambient ionization sources. She received her PhD in Analytical Chemistry from Purdue University where studied under the advisement of Prof. R. Graham Cooks. </p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Dr. Martin Graf-Utzmann (Editor, Wiley Analytical Science, Moderator)</p>
</blockquote>
<blockquote>
<p>Dr. Martin Graf-Utzmann has a Ph.D. in Theoretical Chemistry and is an editor for Wiley Analytical Science. His interests are mainly Laboratory Automation, Digitalization, and Lab Equipment.</p>
</blockquote>


Wiley Analytical Science: Jump Start Your LC/Q-TOF Omics Investigation with Reliable Workflows

Jump Start Your LC/Q-TOF Omics Investigation with Reliable Workflows

This webinar will focus on untargeted LC/MS Omics solutions that will provide the biological insights needed to produce meaningful results.

Your LC/Q-TOF Omics Investigation with Reliable Workflows

<p><strong>This year we invite you to ignite your mind to Be Curious about what Ion chromatography (IC) can do with its versatility in many detections across the IC application spectrum to improve your workflows and solve challenges.</strong></p>
<p>During this three day virtual event, learn from a panel of experts how the latest IC applications are helping colleagues achieve breakthroughs, and walk away with valuable information on how advancements in IC can increase laboratory analytical capabilities. </p>
<p>Although each day is convenient for a specific region, you can attend any session on any day. All sessions and workshops will be available for on-demand viewing after the event concludes.</p>
<h3><strong>Day 1 Agenda | April 18 | North and South America</strong></h3>
<p>Discover IC column development, and where it’s headed with mass spectrometry, as they can be an integral detection for carbohydrate profiling and environmental metabolites characterization. Learn how standalone IC can solve industrial samples and degradation products with comprehensive IC information, all at once.</p>
<h5><strong>11:30 EDT: Opening Plenary: The Past, Present, and Future of IC Column Development</strong></h5>
<ul>
<li>Alexandra Zatirakha (Thermo Fisher Scientific, IC/SP R&amp;D, Sunnyvale)</li>
</ul>
<h5><strong>12:30 EDT: Characterizing Carbohydrate Degradation Products from Bacteroides Thetaiotaomicron to Understand Bacterial Dextran Utilization in the Gut</strong></h5>
<ul>
<li>Neil Rumachik (Thermo Fisher Scientific, IC/SP R&amp;D, Sunnyvale)</li>
<li>Fiona Cuskin (Newcastle University, UK)</li>
</ul>
<h5><strong>1:30 PM EDT: Toward Comprehensive Chemical Characterization of Metabolomic Using Orbitrap Fusion Tribrid Mass Spectrometer Coupled with Ion and Liquid Chromatography Techniques: Dissolved Organic Matter as an Example</strong></h5>
<ul>
<li>Hussain Abdulla (Department of Physical and Environmental Sciences, Texas A&amp;M University-Corpus Christi)</li>
</ul>
<h5><strong>2:30 PM EDT: The Use of Ion Chromatography in the Monitoring of Degradation Products from the Electrochemical Treatment Of Organic Compounds</strong></h5>
<ul>
<li>Emily Tossi (Federal University of Rio Grande do Norte)</li>
</ul>
<h5><strong>3:30 PM EDT: Ion Chromatography as a Tool for Industrial Problem Solving</strong></h5>
<ul>
<li>Isaac Negrete and Stephen Fosdick (Dow)</li>
</ul>
<h5><strong>4:30 PM EDT: Workshop: Everything, Everywhere, All at Once IC!</strong></h5>
<ul>
<li>Kelly Femrite (IC/SP Product Support, Sunnyvale)</li>
<li>Carl Fisher (IC/SP Product Marketing, Sunnyvale)</li>
<li>Criss Corchard-Keeler (Service Marketing Manager, CMD/MOL Thermo Fisher Scientific)</li>
</ul>


Thermo Fisher Scientific: IC Symposium 2023

IC Symposium 2023 - Day 1

Join us for the 2023 Global IC Symposium! North and South America

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


IC Symposium 2023 - Day 3

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

<p><strong>A novel spatial technique, DISCO-MS, combines whole-organ/whole-organism clearing and imaging, deep-learning-based image analysis, robotic tissue extraction, and ultra-high-sensitivity mass spectrometry with the Bruker timsTOF instrument family. This combination enables DISCO-MS to perform unbiased proteome analysis of preclinical and clinical tissues from quantity-limited materials after unbiased imaging of entire specimens in 3D.</strong></p>
<p>In this webinar, you will learn about a new experimental approach that combines whole tissue clearing, dia-PASEF®, and trapped ion mobility spectrometry (TIMS) mass spectrometry to analyze the spatial proteome of complex tissue structures. The webinar will detail how with this technique, researchers were able to:</p>
<ul>
<li>Analyze the proteome of preclinical and clinical tissues after identification of regions of interest using 3D imaging, followed by robotic tissue extraction</li>
<li>Achieve early unbiased detection and characterization of subtle tissue perturbations across pathologies</li>
<li>Benefit from the use of ultra-high sensitivity and robust timsTOF mass spectrometers</li>
</ul>
<h5>Key learning objectives</h5>
<ul>
<li><strong>Discover the new experimental approach that combines whole tissue clearing, dia-PASEF®, and TIMS mass spectrometers can be used to analyze the spatial proteome of complex tissue structures</strong></li>
<li><strong>Understand how researchers were able to analyze the proteome of specific tissue regions following 3D imaging to enable robotic tissue extraction</strong></li>
<li><strong>Learn about the unparalleled sensitivity and robustness the timsTOF platform offers with 4D-Proteomics™ which enables researchers to delve deeper into proteome analysis and gain greater insights</strong></li>
</ul>
<blockquote>
<p><strong>Presenter:</strong> Dr. Harsharan Singh Bhatia (Institute for Tissue Engineering and Regenerative Medicine (iTERM))</p>
</blockquote>
<blockquote>
<p>Dr. Harsharan Singh Bhatia is the Omics technologies team leader at the Institute for Tissue Engineering and Regenerative Medicine (iTERM), Helmholtz Munich. He completed his Ph.D. at the University of Freiburg, Germany, studying the neuroprotective role of dietary antioxidants. Bhatia worked as a postdoctoral researcher at UCLA, where he investigated the impact of dietary manipulations on rodent behavior. He later returned to the University of Freiburg to work as a research associate at the University Clinic, exploring epigenetic factors&#39; regulation of microglial function. In 2017, Bhatia joined iTERM to study chronic neuroinflammation using DISCO tissue clearing and spatial-omics tools.</p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Jemima Arnold (Editorial Team, SelectScience)</p>
</blockquote>
<blockquote>
<p>Jemima studied Cellular and Molecular Medicine at the University of Bristol, UK, and as a member of the Editorial team, she now plays an integral role in shaping the content on SelectScience.</p>
</blockquote>


SelectScience: Spatial proteomics in three-dimensional intact specimens

Spatial proteomics in three-dimensional intact specimens

A new experimental approach that combines whole tissue clearing, dia-PASEF®, and TIMS MS to analyze the spatial proteome of complex tissue structures.

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


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

How to set MS Scan Parameters for your LCMS Experiment

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

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


Targeted Workflows

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

Targeted LC/MS Workflows

<p>Webinar in collaboration with the Polish Society of Metabolomics.</p>
<h3><strong>14:00 - 14:20 Benefits of Trapped Ion Mobility Spectrometry (TIMS) for Metabolomics and Lipidomics</strong></h3>
<ul>
<li><strong>Presenter:</strong> Dr. Stefanie Wernisch ( Business Development Manager Metabolomics/Multiomics, Bruker Daltonics Bremen, Germany)</li>
</ul>
<p>After revolutionizing the area of proteomics, trapped ion mobility spectrometry (TIMS) is now conquering the fields of metabolomics and lipidomics. Bruker&#39;s unique timsTOF technology addresses the complexity of biological samples by adding an orthogonal dimension of separation before mass spectrometric analysis, thus reducing the complexity of MS/MS data and improving annotation confidence for untargeted analysis. The ability to determine Collisional Cross Sections (CCS) can further aid identification and outlier detection in lipidomics studies.</p>
<h3><strong>14:20 - 14:40 SpatialOMx® for in-depth 4D-Lipidomics™</strong></h3>
<ul>
<li><strong>Presenter:</strong> Dr. Janina Oetjen (Application Specialist MALDI Imaging, Bruker Daltonics Bremen, Germany)</li>
</ul>
<p>The combined possibilities of ESI and MALDI in one instrument enables powerful SpatialOMx® applications. In short, ion mobility-based annotation can connect confident LC-TIMS-MS/MS identification with meaningful spatial information from MALDI Imaging, specifically in the field of lipidomics. Further, segmentation results based on lipid imaging can define specific regions of interest for subsequent, in-depth analysis. Thus, the information content of MALDI Imaging can be enhanced with SpatialOMx® workflows on the timsTOF fleX platform.</p>
<h3><strong>14:40 - 15:00 Application Round-up: 4D-Metabolomics™ and 4D-Lipidomics™</strong></h3>
<ul>
<li><strong>Presenter:</strong> Dr. Matthias Szesny (Application Scientist Metabolomics, Bruker Daltonics Bremen, Germany)</li>
</ul>
<p>We will highlight the capabilities of the timsTOF platform and introduce new applications, method developments, and software solutions in the field of metabolomics and lipidomics. Those help scientists gain a faster and deeper understanding of diverse research areas such as health and disease as well as agriculture.</p>


Bruker: Expanding the Horizons of 4D-Metabolomics and 4D-Lipidomics

Expanding the Horizons of 4D-Metabolomics and 4D-Lipidomics

Benefits of TIMS for Metabolomics and Lipidomics. SpatialOMx for in-depth 4D-Lipidomics, Application Round-up: 4D-Metabolomics and 4D-Lipidomics.

LCMS webinars focusing on LC/HRMS - page 40