A team from CEITEC Masaryk University (MUNI) in collaboration with researchers from two research institutes in Norway has, for the first time, captured how echovirus 18, a member of the enterovirus genus, releases its genetic material into cells to initiate infection. The study provides a structural view of an early stage of viral infection under near-native conditions. Using cryo-electron microscopy, the researchers discovered that the virus does not release its RNA through a small pore in its capsid, as had long been assumed. Instead, its protein shell partially disassembles, creating a large opening through which the viral genetic material escapes into the host cell. A detailed understanding of this genome release mechanism could eventually help develop compounds preventing enteroviruses from infecting cells.Enteroviruses are common human pathogens causing diseases ranging from the common cold and gastrointestinal infections to severe neurological disorders. Echovirus 18, the virus investigated in this study, is known primarily as a cause of meningitis and encephalitis in children. It belongs to the picornaviruses, a family of small, non-enveloped viruses whose genetic material is protected by a protein shell, the capsid, organized with icosahedral symmetry.To replicate within a cell, the enteroviruses must release their RNA – the molecule that carries viral genetic information – from the capsid, into the cell cytoplasm. Although this step is crucial for initiating infection, it has never been observed in infected cells.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vedci_z_CEITEC_jako_prvni_zachytili_jak_enteroviry_spousteji_infekci_bunek_71d553bb0e.jpg" alt="CEITEC/Plevka Lab: CEITEC Scientists Are the First to Capture How Enteroviruses Initiate Infection: View into a cell infected by echovirus 18. Echovirus 18 is shown in green and yellow, ribosomes in violet, and actin filaments in cyan. Scale 50 nm. " srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vedci_z_CEITEC_jako_prvni_zachytili_jak_enteroviry_spousteji_infekci_bunek_71d553bb0e.jpg 221w," sizes="100vw" width="1600" height="1128">“For a long time, two main theories existed about how picornaviruses deliver their RNA genomes into cells. One proposed that the genome leaves the capsid through a small opening. The other, supported by earlier work from our laboratory, suggested that the genome escapes from partially disassembled capsids missing pentamers of capsid proteins. However, both models were based on experiments with virus particles outside cells. We wanted to go one step further and see what really happens during infection inside a cell,” says <a target="_blank" rel="noopener noreferrer" href="https://www.ceitec.eu/liya-mukhamedova-ph-d/u89248?page=publication">Liya Mukhamedova</a>, the study’s first author from CEITEC MUNI.Using cryo-electron microscopy, which allows scientists to visualize biological structures at exceptionally high resolution, the researchers observed individual echovirus 18 particles directly within infected cells. They discovered that empty virus particles in infected cells lack parts of their capsids. It is through these openings that the virus releases its RNA.The study also revealed the role of the FcRn receptor, a cell-surface molecule that enteroviruses use to enter cells. The binding of the virus to the receptor triggers structural changes in the viral particle that prime it for subsequent genome release. The team showed that receptor binding causes the loss of the so-called pocket factor, a small molecule that normally helps stabilize the virus particle. The virus otherwise remains largely intact, suggesting that receptor binding is only the first step toward uncoating, while additional factors within the cell are required to complete the process and trigger genome release.“Infection is a complex process, during which enterovirus particles sense various interactions with cell components. The binding of echovirus 18 to the FcRn host-cell receptor triggers conformational changes in the virus, priming it for genome release.” – explains <a target="_blank" rel="noopener noreferrer" href="https://www.ceitec.eu/pavel-plevka-ph-d/u26854">Pavel Plevka</a>, head of the Structural Virology Research Group.The researchers did not observe the so-called activated particles that are key intermediates in the enterovirus uncoating process. This suggests that genome release in cells occurs much faster than previous experiments had suggested.By combining structural data obtained from studies of virus particles outside living cells with observations of infected cells, the study offers a picture of how enterovirus infection begins. Moving beyond simplified experiments with isolated virus particles, it brings scientists closer to understanding the earliest stages of enterovirus infection as they occur in living cells. The study, was published in the <a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1073/pnas.2601182123">PNAS journal</a>.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vedci_z_CEITEC_jako_prvni_zachytili_jak_enteroviry_spousteji_infekci_bunek_2_3601bf1df9.jpg" alt="CEITEC/Plevka Lab: CEITEC Scientists Are the First to Capture How Enteroviruses Initiate Infection: Reconstructions of E18 particles from infected cells. The particles are rainbow-colored based on the distance from the particle center. Scale 10 nm." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vedci_z_CEITEC_jako_prvni_zachytili_jak_enteroviry_spousteji_infekci_bunek_2_3601bf1df9.jpg 245w," sizes="100vw" width="1600" height="906"><blockquote><h4>Article</h4><h4><a target="_blank" rel="noopener noreferrer" href="https://www.pnas.org/doi/10.1073/pnas.2601182123">Particles of echovirus 18 open to release their genomes in vivo</a></h4>Liya Mukhamedova, David Buchta, Zuzana Trebichalská, Yevgen Levdansky, Jana Moravcová, David Potěšil, Zbyněk Zdráhal, Dominik Hřebík, Lucie Nepovímová, Torleif Tollefsrud Gjølberg, Jan Terje Andersen, Jiří Nováček, Tibor Füzik, and Pavel PlevkaProc. Natl. Acad. Sci. U.S.A., 2026, 123, e2601182123<div>&nbsp;</div><div><a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1073/pnas.2601182123">https://doi.org/10.1073/pnas.2601182123</a></div><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>Enteroviruses cause a broad spectrum of human diseases, ranging from mild respiratory or gastrointestinal infections to severe neurological disorders such as aseptic meningitis and encephalitis. Enterovirus cell entry involves receptor-mediated endocytosis followed by destabilizing rearrangements of the virus capsid that enable genome release. However, the mechanism of enterovirus genome release has not been visualized in infected cells. Here, we used cryoelectron tomography and microscopy to image echovirus 18 (E18) entry into host cells and its interaction with the neonatal Fc receptor (FcRn). 30 min postinfection, endosomes and cytoplasm contained empty capsids missing one or several pentamers of capsid proteins, providing evidence that in vivo E18 releases its genome through capsid opening. In vitro, FcRn binding induced the expulsion of pocket factors from hydrophobic pockets in VP1, priming the virus for uncoating. The cryoelectron microscopy reconstruction of genome-containing particles of E18 inside infected cells did not reveal pocket factors, indicating that receptor binding triggers the same priming process during infection. We did not detect activated particles in infected cells, suggesting that these intermediates are short-lived and rapidly release their genomes in vivo. Our results identify capsid opening as the in vivo mechanism of echovirus 18 genome release, providing structural evidence for a process previously only inferred from in vitro experiments.

CEITEC Scientists Are the First to Capture How Enteroviruses Initiate Infection 

Gas chromatography (GC) is a powerful analytical technique used to separate and analyze compounds in a mixture. Whether you're working in pharmaceuticals, environmental testing, or food safety, understanding the key components of a gas chromatograph is essential for accurate and efficient results.In this article, we will delve into the primary components of gas chromatography, including the injector, column, detector, and carrier gas—and explain how each plays a critical role in the separation and analysis process.By mastering these elements, you can optimize your GC setup for precise and reliable outcomes. Let's explore each component in detail:<h3>Sample Injector</h3>The injector is the starting point in the <a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/techniques/gc">gas chromatography process</a>, where the sample is introduced into the system. In GC, the sample must be vaporized into a gas before it enters the column. The injector serves this purpose by heating the sample to its gaseous state. There are many types of injectors, Split/Splitless, PTV, on column.The most common injector is the Split/Splitless injector that can be used in split mode or in splitless mode:<ul><li>Split Injection: This mode allows a portion of the sample to be sent to the column while the remainder is vented. It is useful for high-concentration samples to prevent system overload.</li><li>Splitless Injection: In this mode, the entire sample is introduced into the column, making it ideal for trace analysis where even minute quantities need detection.</li></ul>Proper choice of injector type and proper control of injection conditions, such as temperature, sample size, injection mode are crucial for achieving reproducible and reliable results.<h3>Carrier Gas</h3>In gas chromatography, the mobile phase is represented by carrier gas, which transports the vaporized sample through the column. The carrier gas is an inert gas, such as helium, nitrogen, or hydrogen. The choice of carrier gas can influence the efficiency of the separation process.<ul><li>Helium is the most used carrier gas due to its inertness and high flow rate.</li><li>Hydrogen offers faster analysis times but requires careful handling due to its flammability.</li><li>Nitrogen provides a cheaper solution compared to Helium, although it's slower than helium or hydrogen.</li></ul>The flow rate and pressure of the carrier gas need to be carefully controlled to ensure that the sample moves smoothly through the system and adequate efficiency is generated.<h3>Column/Stationary Phase</h3>The column is the heart of the gas chromatograph, where the actual separation of compounds occurs. <a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/gcms/products?category=7&amp;manufacturerItems=50">GC columns</a> are typically long, thin tubes made from stainless steel or fused silica. They are coated with a stationary phase, which interacts with the components of the sample as they pass through.<ul><li>Packed Columns: These contain small particles of stationary phase material and generally have a larger volume. While they are less efficient than capillary columns, they can be suitable for specific applications.</li><li>Capillary Columns: These thin tubes are coated with a stationary phase, offering higher resolution and faster analysis times due to their smaller diameter.</li></ul>The length, diameter, and type of stationary phase of the column are important factors that affect the efficiency and selectivity of the separation. The choice of stationary phase (polar or non-polar; liquid-coated or solid) affects how different compounds interact with it.As the sample moves through the column, compounds separate based on volatility and their affinity for the stationary phase, resulting in distinct peaks in the chromatogram.<h3>Detector</h3>Once the sample has passed through the column, it reaches the detector, where individual components are identified and measured. There are several types of detectors, each suited to different applications:<ul><li>Flame Ionization Detector (FID): One of the most commonly used detectors in GC. It measures ions produced when organic compounds are burned in a hydrogen-air flame. FID is highly sensitive to a wide range of organic compounds and offers a broad linear dynamic range.</li><li>Thermal Conductivity Detector (TCD): Detects changes in the thermal conductivity of the gas stream as analytes elute from the column. It is a universal, non-destructive detector, but is generally less sensitive than FID.</li><li>Electron capture detector (ECD): A very sensitive and selective detector used to detect chlorinated compounds it is easily contaminated and requires very pure and dry carrier and makeup gases and difficult maintenance.</li><li>Mass Spectrometer (MS): Provides structural information, aiding in both identification and quantification. Requires advanced and trained users and it’s difficult to maintain.</li></ul>The choice of detector depends on the type of analysis being performed and the sensitivity required. Each detector converts physical or chemical changes associated with the analytes into a measurable signal, producing a chromatogram that reflects concentration and retention time.<h3>Data System</h3>Although not a physical part of the chromatograph, the data system plays an integral role in processing and interpreting the signals generated by the detector. Modern gas chromatographs are equipped with software that converts detector signals into chromatograms—visual representations of the separation process. The software allows users to quantify and identify the components of the sample based on retention times and peak areas.<h3>How to Read a Gas Chromatogram?</h3>Interpreting a gas chromatogram involves understanding its essential elements, such as peaks, retention times, and the overall data for qualitative and quantitative analysis.<h4>The Nature of the Sample</h4>Begin by considering the sample's characteristics; different samples, such as environmental pollutants or food components, may exhibit distinct peak patterns. Recognizing the baseline (the flat line representing the signal without analytes) is crucial for identifying peaks accurately. While well-defined peaks indicate successful separation of components, poorly shaped or broad peaks may suggest issues with the separation process. For instance, if a mixture is injected and three peaks are observed, it indicates the presence of three different compounds in the sample. Conversely, when evaluating the purity of a sample, one would anticipate observing a single peak. Ideally, the chromatogram should reflect this expectation, confirming the sample's purity.<h4>The Identity of the Sample</h4>Retention time (Rt) is a critical factor in identifying the compounds present in the sample. Each analyte has a characteristic retention time that can be compared to known standards or literature. To confirm identities, a standard mixture should run alongside the sample; this allows to correlate retention times with specific compounds. If available, utilizing MS in conjunction with gas chromatography (GC-MS) can provide additional structural information, enhancing identification accuracy. With HR-MS or MS-MS detectors, unknown compounds can be identified by matching perfectly the Molecular weight or by matching the fragmentation pattern.<h4>The Amount of Sample</h4>Quantifying analytes involves analyzing peak area or height, which is directly proportional to the concentration of the analyte in the sample. A calibration curve constructed from known concentrations can help relate peak areas to actual concentrations. It is essential to consider the detector’s sensitivity and the limits of detection, as peaks below a certain threshold may not provide reliable quantification.

Basic Principles of Gas Chromatography - Separation and Analysis

ISC 2026 - Day 2

Article

Events

Academy

Science and research

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

Phenomenex is a global technology leader committed to developing novel analytical chemistry solutions that solve the separation and purification challenges of researchers in industrial, government and academic laboratories.

Phenomenex

The International Symposium on Chromatography (ISC) represents the oldest conference series focussing on separation science. ISC symposia have been organised since 1956 in each even year. ISC is internationally recognised as one of the premier meeting series for discussion of all modes of chromatography and separation science with a broad coverage of techniques and applications.

International Symposium on Chromatography - (ISC)

Determination of nitrosamine content (Bioanalytic)

Our offer includes comprehensive development and validation of methods for determination of nitrosamines in pharmaceutical products. We perform the work according to the criteria and needs of the client based on the EMA note.

Determination of nitrosamines is one of the pharmaceutical industry's top priorities. After the presence of N-nitrosodimethylamine (NDMA) was first reported in an active pharmaceutical ingredient (API), the U.S. Food and Drug Administration (FDA) and the European Medicines Agency (EMA) mandated the identification and control of all APIs and finished products in which there is a risk of nitrosamines.The content of nitrosamines in drug products can be controlled primarily by liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) analysis. More than that, a reliable analysis result in our offer consists of a well-chosen sample preparation procedure, a selective and sensitive analytical method, and the experience of the analyst, who selects the best method parameters at the optimization stage.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Determination_of_nitrosamine_content_Bioanalytic_2_ce4f440837.jpg" alt="Bioanalytic: Determination of nitrosamine content." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Determination_of_nitrosamine_content_Bioanalytic_2_ce4f440837.jpg 234w," sizes="100vw" width="1536" height="1024">We have gained experience working with leading pharmaceutical companies. As part of our ongoing work, we have developed analytical methods for small-molecule nitrosamines of 70-150 g/mol. These compounds are mainly formed during manufacturing processes and depend on the presence and type of excipients (e.g. NDBA - N-nitroso-dibutylamine). We have also developed methods for determining molecules with higher nitrosamine drug substance related impurities (NDSRIs). In our work, we focus on achieving the highest possible sensitivity, selectivity and precision. To this end, we individually select the parameters of the methods depending on the composition of the drug and the expected nitrosamines. Due to the above criteria and the required detection limits, we perform nitrosamine impurity determinations using LC-MS/MS kits based on <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=52&amp;search=QTRAP+5500%2B">QTRAP 5500+</a> and <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=52&amp;search=QTRAP+6500%2B">QTRAP 6500+</a> mass spectrometers (<a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?mainauthorItems=55">SCIEX</a>).<blockquote>Our offerOur offer includes comprehensive development and validation of methods for determination of nitrosamines in pharmaceutical products. We perform the work according to the criteria and needs of the client based on the EMA note.At the stage of sample preparation, we focus on:<ul><li>obtaining the highest possible recovery of nitrosamines (matrix purification);</li><li>limiting additional synthesis of impurities (selection of appropriate equipment and reagents);</li><li>ensuring the stability of the sample prepared for LC-MS/MS analysis.</li></ul>During the optimization of the LC-MS/MS method, we solve such problems as:<ul><li>selection of an appropriate internal standard;</li><li>separation of the impurity from the API;</li><li>obtaining the expected sensitivity of the analytical method.</li></ul>Quantitative analysis of nitrosamines requires sensitivity, precision and accuracy, which we provide to our customers.</blockquote><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Determination_of_nitrosamine_content_Bioanalytic_1_d629e00e62.jpg" alt="Bioanalytic: Determination of nitrosamine content." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Determination_of_nitrosamine_content_Bioanalytic_1_d629e00e62.jpg 103w," sizes="100vw" width="1130" height="1710">

Identification of the proteins (Bioanalytic)

We perform proteomic analyses on a state-of-the-art high-resolution ZenoTOF 7600 (SCIEX), in which the Zeno ion trap and EAD (Electron-Activated Dissociation) technology together make a powerful combination.

Protein identification is based on experimental measurement of peptide molecular weights and matching the amino acid sequence of the protein under study with protein sequences deposited in libraries (databases). Two approaches are most commonly used in proteomic studies: top-down and bottom-up. The top-down method involves analyzing full protein sequences. Bottom-up analyses, on the other hand, use digestion of proteins with proteolytic enzymes. The peptides obtained by digestion are analyzed using a mass spectrometer. Each analysis leads to a comparison of experimental data with data obtained by theoretical digestion of proteins described in the database.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Identification_of_the_proteins_Bioanalytic_2_6231b73f0d.jpg" alt="Bioanalytic: Identification of the proteins." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Identification_of_the_proteins_Bioanalytic_2_6231b73f0d.jpg 245w," sizes="100vw" width="1536" height="766"><h4>LC-MS/MS</h4>Tandem mass spectrometers are commonly used to determine protein sequences. They allow ion selection of pseudomolecular peptides and then fragmentation and measurement of the masses of the resulting fragments. Fragmentation using collision induced dissociation(CID ) is an invaluable tool in targeted and untargeted MS/MS analysis of small molecules. It is important to note that in proteomic analysis, data obtained using the aforementioned fragmentation method may leave gaps. For example, spectra obtained by CID fragmentation do not allow unambiguous differentiation of some amino acids: leucine from isoleucine (identical molar masses and CID fragmentation) and lysine from glutamine (very similar masses). For this reason, we perform proteomic analyses on a state-of-the-art high-resolution <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=52&amp;search=+ZenoTOF+7600">ZenoTOF 7600</a> (SCIEX), in which the Zeno ion trap and EAD (Electron-Activated Dissociation) technology together make a powerful combination. It enables the creation of unique fragments to differentiate problematic amino acids and increase the sensitivity and specificity of the analysis.<blockquote>We perform analyses of:<ul><li>samples from solution;</li><li>samples from a gel;</li><li>samples from a complex matrix (by prior arrangement);</li><li>samples from lyophilizer;</li><li>samples previously prepared by the client.</li></ul>Qualitative analysis of proteins includes:<ul><li>To confirm the presence of a protein, the sample is subjected to digestion and the result obtained from experimental data is compared with theoretical data;</li><li>Comparison of experimental data on the masses of peptides included in the analyzed protein with the protein sequences described in the database;</li><li>Analysis and identification of the protein mixture;</li><li>Identification of post translational modifications (PTMs) (we use the tools: Skyline, Spectronaut).</li><li>Reporting of the result including, but not limited to, confirmation of the coverage of the protein sequence obtained in the test sample with the theoretical protein and the list of modified peptides, location and % of modifications.</li></ul>Comparative analyses include:<ul><li>Determining the composition of mixtures;</li><li>Comparison and profiling of sample series - protein identification and trend analysis.</li></ul>Our offer also includes:<ul><li>Support in the planning and execution of studies (the scope is determined individually);</li><li>Assistance in the development of extraction methods from complex matrices - biological fluids, plant tissue, animal tissues (the scope is determined individually);</li><li>Statistical analysis using tools: MarkerView (PCA), GraphPad Prism, Trends, Sciex OS;</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1294">Quantitative analysis of proteins</a>;</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1296">Analysis and characterization of monoclonal antibodies</a>.</li></ul></blockquote><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Identification_of_the_proteins_Bioanalytic_1_97cf8c94b3.jpg" alt="Bioanalytic: Identification of the proteins." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Identification_of_the_proteins_Bioanalytic_1_97cf8c94b3.jpg 117w," sizes="100vw" width="1500" height="2000">

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.

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.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.<h4>rHGH Fragment 176–191</h4>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.Its molecular weight is approximately 1,799 Da. It differs from AOD-9604 in the first amino acid of its sequence.<h4>AOD-9604</h4>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.This structural difference allows the two peptides to be distinguished by LC-MS. The molecular weight of AOD-9604 is approximately 1,815 Da.<h4>Analytical Methods</h4><h5>LC-MS – Identification and Contamination Screening</h5>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.<h5>CHNS – Net Peptide Content Determination</h5>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.Because the sample is combusted during CHNS analysis, the result is not affected by solubility issues that may complicate chromatographic measurement of peptide amount.<h5>HPLC – Peptide Purity Determination</h5>HPLC is used to determine peptide purity and the relative proportion of the main peptide component compared with chromatographically detectable impurities.<h4>What the Analysis Determines</h4><ul><li>Identity of rHGH fragment 176–191 or AOD-9604</li><li>Amount of peptide in the sample</li><li>Net peptide content determined by CHNS</li><li>Peptide purity determined by HPLC</li><li>Presence of other peptides or degradation products detected by LC-MS</li><li>Differentiation between rHGH fragment 176–191 and AOD-9604</li></ul><h4>Analysis Parameters</h4><ul><li>Target compounds: rHGH fragment – somatropin 176–191 and AOD-9604</li><li>CAS number of AOD-9604: 221231-10-3</li><li>Molecular weight of AOD-9604: 1,815 Da</li><li>AOD-9604 sequence: H-Tyr-Leu-Arg-Ile-Val-Gln-Cys(1)-Arg-Ser-Val-Glu-Gly-Ser-Cys(1)-Gly-Phe-OH</li><li>CAS number of rHGH fragment: 66004-57-7</li><li>Molecular weight of rHGH fragment: 1,799 Da</li><li>rHGH fragment sequence: H-Phe-Leu-Arg-Ile-Val-Gln-Cys(1)-Arg-Ser-Val-Glu-Gly-Ser-Cys(1)-Gly-Phe-OH</li><li>Identification method: LC-MS</li><li>Amount determination method: CHNS</li><li>Peptide purity method: HPLC</li><li>Detection limit: less than one twentieth of the usual dosage per vial</li><li>Result format for lyophilizates: mg per vial and peptide purity</li><li>Alternative result format: m/m purity and peptide purity</li><li>Minimum lyophilizate sample: one whole unopened vial containing the lyophilizate</li><li>Minimum raw API powder sample: 30 mg in a sealed glass vial to prevent moisture absorption</li><li>Average turnaround time: 7 business days</li></ul><blockquote><h5>Important Notice</h5>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.</blockquote><h4>Additional Analyses</h4><h5>TFA Analysis</h5><ul><li>Detection and measurement of trifluoroacetic acid (TFA) in the sample. Results are reported in mg per vial.</li></ul><h5>Raw Data</h5><ul><li>Delivery of the available raw analytical data from the primary test and all applicable additional analyses.</li></ul><h5>Fentanyl Presence Analysis</h5><h5>Alternative Result Format – m/m Purity</h5><ul><li>Alternative reporting of the result as mass-by-mass purity. This option is intended exclusively for raw API powders.</li></ul><h5>Variance Testing</h5><ul><li>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.</li></ul><h5>pH Measurement</h5><h5><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/2522">Endotoxin Analysis</a></h5><ul><li>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.</li><li>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.</li><li>Where endotoxin levels above 10 EU per vial are expected, the method can be calibrated for the higher range in advance.</li></ul><h5>Additional Report</h5><ul><li>A separate additional laboratory report issued under a different client name.</li></ul><h5><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/2527">Sterility Testing</a></h5><ul><li>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.</li></ul><h5><a target="_blank" rel="noopener noreferrer" href="https://icpms.labrulez.com/products/2525">Heavy Metals Analysis</a></h5><ul><li>Detection of arsenic, cadmium, lead and mercury in the sample. Testing for other metals can be arranged individually.</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.

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).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.<h4>About the Screening</h4><ul><li>GCMS screening uses the NIST 2014 mass spectral library to identify a broad range of potentially harmful substances in the product. Detection is limited to volatile and semi-volatile compounds and this method is not suitable for peptide samples. &nbsp;</li><li>LCMS screening 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>Both methods provide identification of detected contaminants only. Quantitative determination of a detected substance can be offered separately.<h4>Key Features</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>Analysis Parameters</h4><ul><li>Testing method: GCMS or LCMS</li><li>Amount of sample required: 1 tablet/capsule, 1 ml solution, 200 mg raw material, or 1 vial</li><li>Average turnaround time: 7 business days</li></ul><blockquote>Important Notice<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>Optional Additional Analyses</h4>The following optional laboratory services are available:<ul><li>Additional Laboratory Report</li></ul>

Products from category Pharmaceutical analyses focused on LC/MS - page 1

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