<p><strong>Whether a drug can effectively bind to its target protein, or how different parts of a virus or a cell interact, depends on processes taking place at the level of individual molecules. Their behaviour is determined not only by their shape, but also by the electrostatic forces acting between them. Understanding how these forces are distributed helps scientists explain why certain molecules attract each other, how they bind and how they interact.</strong></p><p>This is where the <a target="_blank" rel="noopener noreferrer" href="https://acc.biodata.ceitec.cz/"><i><strong>Atomic Charge Calculator (ACC)</strong></i></a> comes in. Researchers at Masaryk University have been developing this computational tool for more than a decade. Its third and most advanced generation to date was developed at <strong>CEITEC Masaryk University</strong> and the<strong> Faculty of Science at Masaryk University</strong>, in collaboration with the <strong>Faculty of Informatics at Masaryk University</strong> and <strong>Palacký University Olomouc</strong>.</p><p><strong>ACC III </strong>calculates the electric charges of individual atoms and visualises their distribution directly within three-dimensional molecular structures. It brings together <strong>twenty different calculation methods</strong> in a single environment and can work with a wide range of molecules – from small organic compounds to proteins and other large biomolecular structures.</p><p>A key advantage of <strong>Atomic Charge Calculator III</strong> is that it combines a broad range of computational methods with ease of access. Basic calculations can be performed directly in a web browser, <strong>with no need to install specialised software or register for an account</strong>. The resulting charges can be displayed directly on a 3D model of the molecule. For advanced users and large-scale analyses, the platform also supports automated data processing and allows its computational core to be run locally.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Co_pritahuje_molekuly_Nova_generace_nastroje_z_CEITEC_zviditelnuje_sily_mezi_atomy_d32d7bd2cd.jpg" alt="CEITEC/Biological Data Management and Analysis Core Facility: What Attracts Molecules? A New Generation of a CEITEC Tool Makes the Forces Between Atoms Visible: Oseltamivir bound to influenza virus neuraminidase (blue: positive partial charges, red: negative charges). A strong electrostatic interaction occurs between a negatively charged region of the drug and positively charged regions of the protein." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Co_pritahuje_molekuly_Nova_generace_nastroje_z_CEITEC_zviditelnuje_sily_mezi_atomy_d32d7bd2cd.jpg 140w," sizes="100vw" width="1600" height="1786"></p><h3><strong>Why are scientists interested in the electric charges of atoms?</strong></h3><p>Electrons are not distributed evenly within molecules. Individual atoms can therefore carry different partial electric charges. These charges play an important role in determining how molecules behave towards their surroundings and towards one another.</p><p>Positively and negatively charged regions of molecules can attract each other, while regions with the same charge repel each other. The distribution of these charges therefore helps determine which molecules approach each other, how they orient themselves and how strongly they may bind. In biology, this is important, for example, in molecular recognition or when a drug binds to its target protein. Understanding partial charges therefore helps scientists gain insight into the interactions underlying the behaviour of many molecular systems.</p><p>There is, however, no single universal way to determine partial charges. Different computational methods can produce different values, and the choice of method also depends on how the results will be used. Accurate quantum-chemical calculations can also become very computationally demanding when large numbers of structures are involved. ACC III therefore brings together<strong> empirical methods </strong>that allow these calculations to be performed more quickly and on a large scale.</p><p><i>“From the outset, we designed ACC III to make calculating partial atomic charges as straightforward as possible. Users do not need to install anything or deal with complicated settings – they simply upload a molecule and start the calculation with a single click. The application then suggests suitable methods from the twenty available and can handle both small molecules and large biomolecular structures,”</i> says <a target="_blank" rel="noopener noreferrer" href="https://www.ceitec.eu/tomas-racek-ph-d/u94476?page=publication"><strong>Tomáš Raček</strong></a>, who has been developing and maintaining ACC since 2018.</p><h3><strong>How an antiviral drug binds to an influenza virus protein</strong></h3><p>The authors demonstrate what charge distribution can reveal using the well-known antiviral drug oseltamivir, marketed as Tamiflu. The drug binds to neuraminidase, a protein of the influenza A virus. ACC III can show directly within the three-dimensional structure where positive and negative partial charges are located and how they contribute to the interaction between the drug and the protein.</p><p><i>“The example of oseltamivir clearly shows why it is useful not only to calculate the charges, but also to visualise them directly within the structure. This allows us to see which parts of the two molecules interact electrostatically. The same approach can be used to study many other molecular systems,”</i> explains Tomáš Raček.</p><p><strong>ACC III is not limited to small molecules</strong>. It can also work with proteins and other large biomolecular structures. The authors demonstrate this using a second example: the <strong>SARS-CoV-2 </strong>pore complex. Coronaviruses form these pores during replication in infected cells and use them to transport viral RNA across membranes. Visualising partial charges helps distinguish the parts of the complex that pass through the non-polar environment of the membrane from its more highly charged regions.</p><h3><strong>From calculation straight to a 3D model</strong></h3><p>The new generation of the Atomic Charge Calculator also offers<strong> more advanced visualisation</strong>. It uses Mol*, which allows calculated charges to be mapped directly onto a three-dimensional structure and explored interactively. A visualisation created using ACC III was also selected for the<strong> cover of the special </strong><i><strong>Nucleic Acids Research</strong></i><strong> Web Server Issue</strong>. Created by Tomáš Raček, the cover image shows the distribution of partial charges in a membrane protein system.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Co_pritahuje_molekuly_Nova_generace_nastroje_z_CEITEC_zviditelnuje_sily_mezi_atomy_3_85cc310925.jpeg" alt="CEITEC/Oxford University Press: What Attracts Molecules? A New Generation of a CEITEC Tool Makes the Forces Between Atoms Visible: Cover page in Nucleic Acids Research journal." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Co_pritahuje_molekuly_Nova_generace_nastroje_z_CEITEC_zviditelnuje_sily_mezi_atomy_3_85cc310925.jpeg 124w," sizes="100vw" width="1600" height="2011"></p><p>Results can be downloaded in several standard formats and, for the first time, stored directly in the mmCIF format commonly used for three-dimensional biomolecular structures. Information about the structure and its calculated charges can therefore remain together in a single file and be used by other tools.</p><p>For researchers who need to process large numbers of structures, ACC III also provides an API and a computational core that can be run locally. The platform can therefore be used both for individual calculations through its web interface and as part of larger automated analyses.</p><h3><strong>More than a decade of development</strong></h3><p>Scientists introduced the first Atomic Charge Calculator in <strong>2015</strong>, followed by its second generation in <strong>2020</strong>. In the meantime, the team also developed specialised tools: PDBCharges for structures from the Protein Data Bank and AlphaCharges for structures from the AlphaFold Database.</p><p><i>“The Atomic Charge Calculator was never a one-off project,”</i> says <a target="_blank" rel="noopener noreferrer" href="https://www.ceitec.eu/prof-radka-svobodova-ph-d/u17518?page=publication"><strong>Radka Svobodová</strong></a>, Head of the Biological Data Management and Analysis Core Facility at CEITEC Masaryk University. <i>“For more than a decade, we have been continuously developing tools that respond both to new possibilities in structural bioinformatics and to the needs of their users. The third generation combines straightforward web-based use with capabilities that are important for the automated processing of large numbers of molecular structures.”</i></p><blockquote><p><strong>Atomic Charge Calculator III is freely available through its web interface and does not require registration for basic use.</strong> Its development was supported by the<strong> ELIXIR CZ </strong>research infrastructure.</p></blockquote><h5><strong>The authors presented the new generation of the tool in </strong><a target="_blank" rel="noopener noreferrer" href="https://academic.oup.com/nar/article/54/W1/W211/8662890"><i><strong>Nucleic Acids Research</strong></i></a><strong>.</strong></h5>

What Attracts Molecules? A New Generation of a CEITEC Tool Makes the Forces Between Atoms Visible 

<p><span><strong>Not every concentration job can tolerate heat — and not every concentrator that handles heat well can handle cold. </strong></span><a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/all/products/2441"><span><strong>Refrigerated centrifugal vacuum concentrators</strong></span></a><span><strong> exist for a specific reason: proteins, RNA, enzymes, and synthetic peptides degrade quickly under thermal stress, and standard concentrators that rely on heat alone can compromise sample integrity before evaporation finishes. We compared two of the leading refrigerated systems — the Labconco Refrigerated CentriVap and the </strong></span><a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/all/products/2611"><span><strong>Thermo Fisher Refrigerated SpeedVac SRF110</strong></span></a><span><strong> — to see how they stack up for labs where sample preservation is non-negotiable.</strong></span></p><blockquote><p><a target="_blank" rel="noopener noreferrer" href="https://explore.organomation.com/labconco-refrigerated-centrivap-vs-thermo-fisher-refrigerated-speedvac"><span><strong>Download the full comparison with pricing here!</strong></span></a></p></blockquote><h3><strong>The Problem Refrigeration Actually Solves</strong></h3><p>It's a detail that gets lost in most spec-sheet comparisons: running a<a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/lcms/products?manufacturerItems=540&amp;search=centrivap"><strong> vacuum concentrator </strong></a>without temperature control can cause a sample to over-cool itself. As solvent evaporates under vacuum, the process pulls latent heat from the sample — the same evaporative cooling effect that makes sweat feel cold on skin. For a heat-stable solvent, that's irrelevant. For a temperature-sensitive biomolecule, it can drop the sample low enough to risk unwanted freezing or sublimation mid-run. Labconco's own engineering notes for the Refrigerated CentriVap describe this directly: the unit pairs a refrigeration system with a heater so operators can hold a precise set-point temperature and avoid sublimated samples caused by evaporative cooling. That's the whole reason this product category exists, and it's worth understanding before comparing specs line by line.</p><h3><strong>Price: A Wider Gap at the High End</strong></h3><p>The <strong>Labconco Refrigerated CentriVap</strong> is typically priced around <strong>$13,000 USD</strong>. The <strong>Thermo Fisher SRF110</strong> runs higher, generally<strong> $15,000–$17,000 USD</strong>, and that's before factoring in the modular kit components — Thermo Fisher sells the SRF110 with a separate vacuum system, rotor, vapor trap, and heat transfer fluid bundled into the total kit price. The price gap between these two refrigerated units is proportionally larger than what we found comparing their non-refrigerated counterparts, which makes the value case for the CentriVap even more pronounced at this tier.</p><h3><strong>Capacity: The Difference That Matters Most Right Now</strong></h3><p>This is where the two systems really separate, and it lines up with where lab demand is heading. The Refrigerated CentriVap processes up to <strong>312 samples</strong> per run; the SRF110 tops out at <strong>132</strong>. Both handle volumes up to 50 mL, so this isn't a volume trade-off the way it was in our earlier comparison — it's a straight throughput advantage for the CentriVap.</p><p>That gap matters because<a target="_blank" rel="noopener noreferrer" href="https://peptidestaff.com/industry-trends/peptide-therapy-market-forecast-2026/"><strong> peptide-based therapeutics </strong></a>have become one of the fastest-growing classes of drugs in the pharmaceutical industry, and manufacturing capacity — not demand — is widely cited as the primary bottleneck holding the sector back. <a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/all/article/7541"><strong>GLP-1 programs</strong></a> in particular are pushing <a target="_blank" rel="noopener noreferrer" href="https://www.bachem.com/knowledge-center/glp-1-demand-for-peptide-manufacturers/"><span><strong>peptide manufacturers</strong></span></a><span> </span>toward industrialized, large-scale production platforms rather than one-off batch work. <a target="_blank" rel="noopener noreferrer" href="https://www.organomation.com/"><strong>Sample prep equipment</strong></a> sits squarely inside that bottleneck: every purification run, HPLC fraction, and concentration step has to scale alongside the chemistry. A concentrator that processes more than double the samples per run, like the Refrigerated CentriVap, is a meaningfully different proposition for a peptide synthesis or purification lab than it would have been five years ago.</p><h3><strong>Temperature Range: How Cold You Can Go</strong></h3><p>The CentriVap's refrigeration reaches as low as<strong> -10°C</strong>; the SRF110 bottoms out at <strong>-4°C</strong>. Both units heat up to +100°C. That six-degree gap on the cold end isn't dramatic on paper, but for the most heat-labile peptides and enzymes, the lower floor gives operators more margin before a sample is at risk — particularly during longer runs where evaporative cooling has more time to compound any thermal load on the sample.</p><h3><strong>Vortex Speed and Mechanical Flexibility</strong></h3><p>The CentriVap offers an adjustable vortex range from <strong>500 to 1,800 rpm</strong>, while the SRF110 runs up to<strong> 1,725 rpm</strong>. The CentriVap's lower floor is the more useful distinction here — fragile, large, or shear-sensitive samples (think intact proteins or larger peptide constructs) sometimes need to run at reduced rotor speed to avoid mechanical stress, and the CentriVap gives operators that headroom on both ends rather than just a ceiling.</p><h3><strong>Lid Material: Visibility vs. Durability</strong></h3><p>The Refrigerated CentriVap uses a <strong>glass lid</strong>, letting operators see into the chamber during a run. The SRF110 uses an <strong>epoxy-coated aluminum lid</strong>, which trades visibility for added durability. For labs running visually distinct sample batches — colored buffers, multiple project codes, HPLC fractions pulled at different time points — the ability to glance at the chamber without interrupting a run has real workflow value, especially in a core facility setting where one instrument serves multiple research groups.</p><h3><strong>What This Means for Core Facilities</strong></h3><p>Shared instrumentation cores feel throughput and cold-temperature constraints differently than a single-PI lab does. A<a target="_blank" rel="noopener noreferrer" href="https://blog.organomation.com/blog/an-appreciation-for-academic-core-labs"><strong> core running samples from multiple research groups </strong></a>— some doing routine RNA cleanup, others running heat-labile peptide fractions from an HPLC purification step — needs an instrument that won't bottleneck on either axis. The CentriVap's combination of higher per-run capacity and a lower refrigeration floor gives a shared facility more room to serve mixed workloads without forcing every group onto the same conservative settings a less flexible unit would require.</p><h3><strong>Built for the Same Footprint</strong></h3><p>Both units are sized for fume hood placement, with the CentriVap measuring<strong> 15.0 x 27.2 x 13.9 inches </strong>against the SRF110's<strong> 16.62 x 25 x 13.75 inches </strong>— close enough that floor planning isn't a deciding factor either way. Both carry <strong>standard one-year warranties</strong>.</p><h3><strong>The Bottom Line</strong></h3><p>For labs concentrating proteins, RNA, enzymes, or peptide fractions at scale — particularly anyone supporting peptide therapeutic development, where production capacity is already the limiting factor industry-wide — the Labconco Refrigerated CentriVap's combination of higher throughput, lower cold-temperature floor, and lower price makes it the stronger fit. The SRF110 remains a capable option for labs with smaller batch sizes already standardized on Thermo Fisher's modular vacuum ecosystem.</p><p>Organomation distributes the full Labconco CentriVap line, including the Refrigerated and Refrigerated Pro models. Contact our team at sales@organomation.com to talk through rotor configuration, cold trap pairing, and throughput planning for your lab.&nbsp;</p><blockquote><h5><a target="_blank" rel="noopener noreferrer" href="https://explore.organomation.com/labconco-refrigerated-centrivap-vs-thermo-fisher-refrigerated-speedvac"><span><strong>Download the full comparison with pricing here!</strong></span></a></h5></blockquote>

Refrigerated SpeedVac SRF110 vs. CentriVap - Why Sample Capacity Matters More Than Ever for Peptide and Protein Labs

<p><strong>Our Library never stops expanding. What are the most recent contributions to LabRulezLCMS Library in the week of 14th September 2026? Check out new documents from the field of liquid phase, especially HPLC and LC/MS techniques!</strong></p><blockquote><p><span style="font-size:20px;">👉 </span><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library"><span style="font-size:20px;"><strong>SEARCH THE LARGEST REPOSITORY OF DOCUMENTS ABOUT LCMS AND RELATED TECHNIQUES</strong></span></a></p></blockquote><blockquote><p><strong>👉 Need info about different analytical techniques?</strong> Peek into <a target="_blank" rel="noopener noreferrer" href="https://gcms.labrulez.com/library"><strong>LabRulezGCMS</strong></a> or <a target="_blank" rel="noopener noreferrer" href="https://icpms.labrulez.com/library"><strong>LabRulezICPMS</strong></a> libraries.</p></blockquote><p>This week we bring you application notes by <strong>Agilent Technologies </strong>and <strong>Waters Corporation </strong>and posters by <strong>Shimadzu / AOAC </strong>and<strong> Thermo Fisher Scientific / Metabolomics!</strong></p><h3><strong>1. Agilent Technologies: Improved Analysis of Intact Proteins and Peptides by Reversed Phase HPLC Using the Altura Ultra Inert PLRP-S 1000 Å Column</strong></h3><ul><li>Application note</li><li><a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/pdf/an_altura_ultrainert_column_HPLC_analysis_5994_9322en_agilent_2b3a542647.pdf"><strong>Full PDF for download</strong></a></li></ul><p>Intact protein analysis by reversed-phase HPLC (RP-LC) plays a vital role in quality control for determining the purity of biotherapeutic proteins and improving the identification and quantification of critical quality attributes (CQAs). When coupled to mass spectrometric detection, it allows several things. First, an accurate molecular weight to be determined; second, the identification of variants containing post‑translational modifications (PTMs) and proteoforms; and third, the antibody-to-drug ratio in the case of antibody drug conjugates (ADCs).<sup>1</sup>&nbsp;</p><p>While many RP columns have a silica-based stationary phase to enable broader functionalization, residual acidic silanol groups can interact with basic residues in peptides, proteins, and other biomolecules, resulting in significant peak tailing and loss of chromatographic performance. Polystyrene/divinyl benzene (PS/DVB)-based stationary phases do not contain unintentional adsorption sites. Additionally, larger pore sizes have demonstrated superior chromatographic efficiency through less diffusion restriction into the pore volume and reduction of size exclusion mechanisms, degrading the RP-based selectivity.<sup>2</sup>&nbsp;</p><p>Wide-pore columns like the PLRP-S 1000Å provide an exceptional performance with biomolecules, particularly when combined with MS-compatible mobile phase conditions such as formic acid.&nbsp;</p><p>Even so, some undesirable interactions may be observed when using stainless-steel column hardware. Molecules that possess multiple negative charges (including oligonucleotides, phosphorylated peptides and proteins, and proteins with low isoelectric point in general) may interact with exposed metal ions in stainless-steel column hardware. This can result in the need to "deactivate" new columns by making multiple injections of sample until reproducible results are obtained.&nbsp;</p><p>This application note demonstrates how the new <a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/lcms/library?mainauthorItems=10&amp;search=Altura+Ultra+Inert"><strong>Altura Ultra Inert </strong></a>PLRP-S 1000 Å column serves as an effective high-performance workhorse in the analysis of large, intact biomolecules. Developed to effectively block nonspecific adsorption during separations, Ultra Inert technology reduced passivation time 15-fold and delivered ~ 10% greater recovery for mAbs and ADCs and up to 100% for smaller biomolecules like GLP-1s and small globular proteins.</p><h4><strong>Experimental</strong></h4><h5><strong>Instrumentation&nbsp;</strong></h5><ul><li>Agilent 1290 Multicolumn thermostat (G7116B)&nbsp;</li><li>Agilent 1290 Bio multisampler (G7137A)&nbsp;</li><li>Agilent 1290 Bio high-speed pump (G7132A)&nbsp;</li><li><a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/lcms/library?mainauthorItems=10&amp;search=6530"><strong>Agilent 6530 Q-TOF MS system</strong></a>&nbsp;</li></ul><h5><strong>Software and data processing&nbsp;</strong></h5><ul><li><a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/lcms/library?mainauthorItems=10&amp;search=MassHunter+Workstation"><strong>Agilent MassHunter Workstation, version 10.1&nbsp;</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/lcms/library?mainauthorItems=10&amp;search=MassHunter+Qualitative+Analysis"><strong>Agilent MassHunter Qualitative Analysis software, version&nbsp;B.07&nbsp;</strong></a></li><li>Agilent DAR calculator, version B01.01</li></ul><h4><strong>Conclusion&nbsp;</strong></h4><p>Intact mass analysis is a critical methodology to determine the purity of biotherapeutics, but due to the chemical complexity of these analytes, nonspecific adsorption from both silica stationary phase and metal column housing can be highly deleterious to separation performance. The Agilent Altura PLRP-S 1000 Å provides a highly robust solution combining the chemical inertness of polystyrene/divinyl benzene stationary phase with the ultra‑inert Altura hardware to dramatically reduce deleterious peak tailing and increase recovery for biotherapeutics. Herein, we see that analyte recovery for both mAbs, ADCs, GLP-1s, and globular proteins are improved versus stainless-steel, while the Altura PLRP-S column is capable of monitoring both quality critical PTMs such as loss of drug payload as well as accurate quantification of ADC DAR.</p><h3><strong>2. Shimadzu / AOAC: Ambient Ionization Mass Spectrometric Detection of Aroma Released During Gummy Chewing</strong></h3><ul><li>Poster</li><li><a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/pdf/aoac_2026_47_2_34c41f762f.pdf"><strong>Full PDF for download</strong></a></li></ul><p>In recent years, there has been growing interest in evaluating flavor using analytical instrumentation, and retronasal aroma during eating is important. In this study, we proposed an analytical method for measuring retronasal aroma during eating using a single quadrupole mass spectrometer (<a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/lcms/library?mainauthorItems=1&amp;search=2050"><strong>LCMS-2050</strong></a>) equipped with an ambient ion source (Dark Current Discharge Ionization : DCDI) without pretreatment.</p><h4><strong>Conclusion</strong></h4><p>We developed a simple method for evaluating retronasal aroma using a single quadrupole mass spectrometer with an ambient ionization source. Ambient ionization mass spectrometry (DCDI LCMS-2050) can rapidly measure retronasal aroma during eating. Time-resolved visualization reveals texture-dependent differences in aroma release dynamics among grape-flavored gummies. It is also expected to lead to the visualization of the marriage between food and alcohol. This approach may facilitate objective evaluation of flavor release during consumption and support product formulation and sensory science.</p><h3><strong>3. Thermo Fisher Scientific / Metabolomics: Orbitrap Tribrid Real-Time similarity searching of mzCloud library for guided unknown characterization of tea metabolites</strong></h3><ul><li>Poster</li><li><a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/pdf/po_004849_lsms_rtls_tribrid_apex_small_molecule_metabolomics_po004849_na_en_d0d3156065.pdf"><strong>Full PDF for download</strong></a></li></ul><p>In metabolomics LC-MS data is processed to generate a list of detected compounds with a level of confidence in the identity of each compound based on reference data. This reference data may be spectral data and/or retention time information stored in a library or in silico information generated based on fragmentation rules. These annotated compounds are then used to evaluate biological changes between normal and disease states. One of the major hurdles between collected data and coming to reliable conclusions about the biology is the limited number of standards available to build these libraries. It is common to have hundreds to thousands of compounds detected in a data set that have no library match because there is no commercial standard for that unknown. Instead, there is just an elemental formula and matches from a structure database. These structures can be compared using in silico fragmentation techniques to determine which isomers plausibly match the data. MSn data can help reduce the list of possible matches, but without guidance, ddMS3 may not consistently collect data on the most relevant MS2 fragments to accomplish this.&nbsp;</p><p>In this work we use Real-Time Library Search (RTLS) in a ddMS3 method to help guide the instrument in real time to collect the most relevant data for confirming structural matches.</p><h4><strong>Materials and methods</strong></h4><h5><strong>Test method(s)&nbsp;</strong></h5><p>1 μL aliquots were analyzed using a <a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/lcms/products?category=48&amp;manufacturerItems=3&amp;search=gold"><strong>Thermo Scientific Hypersil GOLD column</strong></a> on a <a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/all/products/744"><strong>Thermo Scientific Vanquish Horizon UHPLC</strong></a><strong> </strong>coupled with a <a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/all/products/561"><strong>Thermo Scientific Orbitrap IQ-X Tribrid mass spectrometer</strong></a> and <strong>Thermo Scientific Orbitrap Tribrid Apex Small Molecule mass spectrometer</strong>. RTLS was run in similarity mode using the offline version of <a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/all/products/1764"><strong>Thermo Scientific mzCloud library</strong></a>.&nbsp;</p><h5><strong>Data analysis&nbsp;</strong></h5><p>Data was processed using <strong>Thermo Scientific Freestyle and </strong><a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/all/products/1759"><strong>Compound Discoverer software</strong></a><strong>.</strong></p><h4><strong>Conclusions&nbsp;</strong></h4><p>Tea extracts were analyzed using RTLS to find the most similar compound in the offline version of the mzCloud library and trigger MS3 on the highest m/z matching and non-matching fragments. This provided additional information to confirm similarity and provide insight on shared sub-structures to the library compound as well as additional information on the portions of the structure that were unique to the experimental compound.</p><h3><strong>4. Waters Corporation: The Quantification of Glucagon-like Peptide Receptor Agonists (GLP-1 RAs) in Plasma Extracts Using Capillary UHPLC-MS/MS</strong></h3><ul><li>Application note</li><li><a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/pdf/720009537_en_0068921516.pdf"><strong>Full PDF for download</strong></a></li></ul><div><div><section><div><div><div><div><div><div><h5><strong>Benefits&nbsp;</strong></h5><ul><li>10-fold improvement in sensitivity&nbsp;</li><li>Robust methodology for &gt;500 injections&nbsp;</li><li>Reduced solvent usage&nbsp;</li><li>No need for complex nanospray MS source</li></ul><p>Obesity represents, perhaps, the largest healthcare challenge, affecting approximately 1.3 billion people globally, contributing to a diverse range of chronic diseases e.g., metabolic, cardiovascular, muscular skeletal, and multiple cancers.1 The rapid growth of obesity and associated global healthcare costs means there is a critical need for safe effective treatments.2 GLP-1 RA initially developed for type 2 diabetes have shown clinical efficacy as weight loss medicines.2 These drugs mimic the action of gut hormones which regulate energy metabolism and appetite by interacting with the hypothalamus, brain stem etc., resulting in weight loss. The success of these GLP-1 RAs is associated with their on-target efficacy and long duration of action,3 e.g., half-life of semaglutide t½ = 160–180 hours3 cf. 1–2 minutes for human GLP-1.4 The long half-life of these GLP-1 RAs results in low, sub ng/mL plasma levels 48–72 hours after dosing, which requires a high sensitivity bioanalytical assay to accurately quantify the plasma concentrations5 and define the PK elimination phase.&nbsp;</p><p>Tandem quadrupole electrospray ionization (ESI) mass spectrometry, operated in multiple reaction monitoring (MRM) mode, coupled with 2.1 mm ID ultra-high performance liquid chromatography (UHPLC) is the dominant technology platform for quantitative bioanalysis. As next generation GIP/GLP-1 RAs promise to be more potent, resulting in lower dosing levels and plasma levels, there is a need for more sensitive analytical methodologies to support drug metabolism and pharmacokinetics (DMPK) studies. Capillary/nano LC-MS/MS have been extensively employed in proteomics to increase analytical sensitivity and enable small volume analysis.5 This sensitivity increase is derived from a combination of the superior ionization efficiency at low flow rates and analyte concentration due to the smaller column geometry.6 This application note illustrates the use of capillary (300 µm) UHPLC-MS/MS (MRM) to affect 10-fold improvement in GLP-1-RAs peak response in human plasma extracts, and detection limits as low as 20 pg/mL for tirzepatide.</p><h4><strong>Experimental</strong></h4><p>Capillary chromatography was performed on an <strong>ACQUITY™ M-class Chromatography System</strong> connected to a <a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/all/products/195"><strong>Xevo™ TQ-XS Mass Spectrometer</strong></a> (Waters Corporation, Wilmslow, UK) equipped with a microflow probe. Capillary UHPLC separations were performed on an <a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/all/products/1952"><strong>ACQUITY Premier Peptide CSH C18</strong></a>, 300 Å, 1.7 µm, 300 µm x 50 mm Chromatography Column.</p><p>MS analysis was performed at unit mass resolution using positive ESI at a capillary voltage of 3.0 kV, with a cone voltage of 32 V. The cone gas flow, desolvation gas flow, and desolvation gas temperature were 50 L/h, 300 L/h and 600 °C, respectively. The data were analyzed using <a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/all/products/1544"><strong>waters_connect™ Software</strong></a><strong>,</strong> and MRM transitions used to monitored for the MS/MS detection of liraglutide, exenatide, semaglutide and tirzepatide were as follows: liraglutide 938.7 → 1128.4, exenatide 838 → 396, semaglutide 1029.2 → 1238.1, and tirzepatide 1204.2 → 396.2. Data analysis was performed using <strong>MS Quan Software.</strong></p><h4><strong>Conclusion</strong></h4><p>Bioanalysis plays a critical role in the drug discovery and development processes providing data to support DMPK, safety assessment, pharmacokinetics/pharmacodynamics (PK/PD), and clinical development studies. The development of new, more potent medicines, innovating delivery platforms, micro sampling, and new approach methodologies (e.g., organ on a chip) all require greater levels of analytical sensitivity. Capillary scale UHPLCMS/MS offers the potential to improve bioanalytical detection limits up to 10-fold, without the need for long analysis times and complex operation associated with nano spray LC-MS/MS. Here, the application of capillary (300 µm ID) scale chromatography for the detection of GLP-1 RAs in human plasma extracts at levels as low as 20 pg/mL with robustness over 500 injections was demonstrated.</p></div></div></div></div></div></div></section></div></div>

News from LabRulezLCMS Library - Week 38, 2026

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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.

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

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rHGH fragment or AOD-9604 (LCMS+CHNS) analysis

Combined LC-MS, CHNS and HPLC analysis of rHGH fragment 176–191 and AOD-9604 for identification, amount, peptide purity and contamination screening.

<p><span><strong>This analysis is designed to identify and determine the amount and purity of recombinant Human Growth Hormone fragment 176–191 and AOD-9604. It combines LC-MS, CHNS and HPLC to provide information about peptide identity, net peptide content, peptide purity and potential contamination with other peptides or degradation products.</strong></span></p><p><span>The test can detect and measure either target compound. It is therefore not necessary to know in advance whether the sample contains rHGH fragment 176–191 or AOD-9604.</span></p><h4><span><strong>rHGH Fragment 176–191</strong></span></h4><p><span>rHGH fragment 176–191, also known as somatropin 176–191, is a peptide corresponding to amino acids 176 to 191 of Human Growth Hormone. It consists of 16 amino acids and represents the C-terminal region of the HGH molecule.</span></p><p><span>Its molecular weight is approximately 1,799 Da. It differs from AOD-9604 in the first amino acid of its sequence.</span></p><h4><span><strong>AOD-9604</strong></span></h4><p><span>AOD-9604 is a synthetically modified peptide derived from Human Growth Hormone fragment 176–191. Like the rHGH fragment, it contains 16 amino acids, but its sequence begins with tyrosine instead of phenylalanine.</span></p><p><span>This structural difference allows the two peptides to be distinguished by LC-MS. The molecular weight of AOD-9604 is approximately 1,815 Da.</span></p><h4><span><strong>Analytical Methods</strong></span></h4><h5><span><strong>LC-MS – Identification and Contamination Screening</strong></span></h5><p><span>LC-MS is used to confirm the identity of the peptide in the sample. It also provides screening for detectable contamination with other peptides and peptide degradation products.</span></p><h5><span><strong>CHNS – Net Peptide Content Determination</strong></span></h5><p><span>CHNS elemental analysis measures the carbon, hydrogen, nitrogen and sulphur content of the sample. The measured values can be used to determine Net Peptide Content.</span></p><p><span>Because the sample is combusted during CHNS analysis, the result is not affected by solubility issues that may complicate chromatographic measurement of peptide amount.</span></p><h5><span><strong>HPLC – Peptide Purity Determination</strong></span></h5><p><span>HPLC is used to determine peptide purity and the relative proportion of the main peptide component compared with chromatographically detectable impurities.</span></p><h4><span><strong>What the Analysis Determines</strong></span></h4><ul><li><span>Identity of rHGH fragment 176–191 or AOD-9604</span></li><li><span>Amount of peptide in the sample</span></li><li><span>Net peptide content determined by CHNS</span></li><li><span>Peptide purity determined by HPLC</span></li><li><span>Presence of other peptides or degradation products detected by LC-MS</span></li><li><span>Differentiation between rHGH fragment 176–191 and AOD-9604</span></li></ul><h4><span><strong>Analysis Parameters</strong></span></h4><ul><li><span><strong>Target compounds:</strong> rHGH fragment – somatropin 176–191 and AOD-9604</span></li><li><span><strong>CAS number of AOD-9604:</strong> 221231-10-3</span></li><li><span><strong>Molecular weight of AOD-9604:</strong> 1,815 Da</span></li><li><span><strong>AOD-9604 sequence:</strong> H-Tyr-Leu-Arg-Ile-Val-Gln-Cys(1)-Arg-Ser-Val-Glu-Gly-Ser-Cys(1)-Gly-Phe-OH</span></li><li><span><strong>CAS number of rHGH fragment:</strong> 66004-57-7</span></li><li><span><strong>Molecular weight of rHGH fragment:</strong> 1,799 Da</span></li><li><span><strong>rHGH fragment sequence:</strong> H-Phe-Leu-Arg-Ile-Val-Gln-Cys(1)-Arg-Ser-Val-Glu-Gly-Ser-Cys(1)-Gly-Phe-OH</span></li><li><span><strong>Identification method:</strong> LC-MS</span></li><li><span><strong>Amount determination method:</strong> CHNS</span></li><li><span><strong>Peptide purity method:</strong> HPLC</span></li><li><span><strong>Detection limit:</strong> less than one twentieth of the usual dosage per vial</span></li><li><span><strong>Result format for lyophilizates:</strong> mg per vial and peptide purity</span></li><li><span><strong>Alternative result format:</strong> m/m purity and peptide purity</span></li><li><span><strong>Minimum lyophilizate sample:</strong> one whole unopened vial containing the lyophilizate</span></li><li><span><strong>Minimum raw API powder sample:</strong> 30 mg in a sealed glass vial to prevent moisture absorption</span></li><li><span><strong>Average turnaround time:</strong> 7 business days</span></li></ul><blockquote><h5><span><strong>Important Notice</strong></span></h5><p><span>The alternative m/m purity result format is intended exclusively for raw API powders. For lyophilized samples, the standard result format provides the peptide amount in mg per vial together with peptide purity.</span></p></blockquote><h4><span><strong>Additional Analyses</strong></span></h4><h5><span><strong>TFA Analysis</strong></span></h5><ul><li><span>Detection and measurement of trifluoroacetic acid (TFA) in the sample. Results are reported in mg per vial.</span></li></ul><h5><span><strong>Raw Data</strong></span></h5><ul><li><span>Delivery of the available raw analytical data from the primary test and all applicable additional analyses.</span></li></ul><h5><span><strong>Fentanyl Presence Analysis</strong></span></h5><h5><span><strong>Alternative Result Format – m/m Purity</strong></span></h5><ul><li><span>Alternative reporting of the result as mass-by-mass purity. This option is intended exclusively for raw API powders.</span></li></ul><h5><span><strong>Variance Testing</strong></span></h5><ul><li><span>Analysis of multiple sample units to assess variation within a single batch. All submitted samples must originate from the same batch of the same product.</span></li></ul><h5><span><strong>pH Measurement</strong></span></h5><h5><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/2522"><span><strong>Endotoxin Analysis</strong></span></a></h5><ul><li><span>Measurement of bacterial endotoxins, particularly lipopolysaccharides (LPS), in the sample. This analysis is available only for finished products and should not be ordered for raw powders.</span></li><li><span>The standard test provides accurate results up to 10 EU per vial. Values above 10 EU per vial are estimated and require an additional test with a different dilution for precise determination. Sending two vials is therefore recommended.</span></li><li><span>Where endotoxin levels above 10 EU per vial are expected, the method can be calibrated for the higher range in advance.</span></li></ul><h5><span><strong>Additional Report</strong></span></h5><ul><li><span>A separate additional laboratory report issued under a different client name.</span></li></ul><h5><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/2527"><span><strong>Sterility Testing</strong></span></a></h5><ul><li><span>TAMC and TYMC testing checks the product for the presence of bacteria, yeasts and moulds. Additional unopened sample units must be submitted for analysis. The average turnaround time for this test is 14 days.</span></li></ul><h5><a target="_blank" rel="noopener noreferrer" href="https://icpms.labrulez.com/products/2525"><span><strong>Heavy Metals Analysis</strong></span></a></h5><ul><li><span>Detection of arsenic, cadmium, lead and mercury in the sample. Testing for other metals can be arranged individually.</span></li></ul>

GCMS/LCMS screening for contamination

GCMS/LCMS screening for identification of contaminants in samples, with the analytical method selected according to sample type.

<p><strong>The GCMS/LCMS Screening for Contamination is a standalone laboratory service designed to identify potential contaminants in a sample using either gas chromatography–mass spectrometry (GCMS) or liquid chromatography–mass spectrometry (LCMS).</strong></p><p>The appropriate analytical method depends on the sample type. GCMS is used primarily for volatile and semi-volatile compounds, while LCMS is suitable for peptide-related contamination.</p><h4><strong>About the Screening</strong></h4><ul><li><strong>GCMS screening</strong> uses the <strong>NIST 2014 </strong>mass spectral library to identify a broad range of potentially <span style="font-weight:400;">harmful substances in the product</span>. Detection is limited to volatile and semi-volatile compounds and this method is not suitable for peptide samples.<br>&nbsp;</li><li><strong>LCMS screening</strong> is intended for peptide products and can detect contamination with other peptides or degraded peptide. Detection is limited to peptides included in the laboratory’s available reference list.</li></ul><p>Both methods provide identification of detected contaminants only. Quantitative determination of a detected substance can be offered separately.</p><h4><strong>Key Features</strong></h4><ul><li>Standalone contamination screening by GCMS or LCMS</li><li>Analytical method selected according to sample type</li><li>GCMS screening for volatile and semi-volatile contaminants</li><li>GCMS identification using the NIST 2014 mass spectral library</li><li>LCMS screening for peptide contamination and degraded peptide</li><li>Identification of detected contaminants</li><li>Quantitative determination available separately after identification</li><li>Suitable for tablets, capsules, liquid solutions, raw materials, and vials depending on the selected method</li><li>Average turnaround time of 7 business days</li></ul><h4><strong>Analysis Parameters</strong></h4><ul><li><strong>Testing method: </strong>GCMS or LCMS</li><li><strong>Amount of sample required: </strong>1 tablet/capsule, 1 ml solution, 200 mg raw material, or 1 vial</li><li><strong>Average turnaround time: </strong>7 business days</li></ul><blockquote><p><strong>Important Notice</strong></p><ul><li>The analytical method is selected according to the type of sample and the expected contaminants.</li><li>GCMS detection is limited to volatile and semi-volatile compounds and cannot be used for peptide samples.</li><li>LCMS detection is limited to peptides included in the laboratory’s available reference list.</li><li>Both GCMS and LCMS screening provide identification only. Quantitative determination of a detected contaminant is not included in the standard analysis and can be offered separately.</li></ul></blockquote><h4><strong>Optional Additional Analyses</strong></h4><p>The following optional laboratory services are available:</p><ul><li>Additional Laboratory Report</li></ul>

Products focused on LC/MS - page 1

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News from LabRulezLCMS Library - Week 38, 2026