Meeting EU Drinking Water Standards: The Critical Role of Sample Prep in Trace Contaminant Analysis

Although modern agriculture needs to be based on accurate real-time data on soil, plant, and environmental conditions, affordable, sufficiently sensitive, and robust monitoring devices for this purpose are currently missing. According to scientists, low-cost sensors based on new smart materials and printing technologies offer a suitable solution. The results of multidisciplinary research thus far and proposals for the development of these devices have been presented by researchers from Czechia, Great Britain, Spain, and the USA in a review article in the prestigious journal <a target="_blank" rel="noopener noreferrer" href="https://www.nature.com/articles/s41467-026-68778-6#Abs1">Nature Communications</a>.“Sensor technologies for monitoring plant health are still in their infancy. Only simple sensors capable of monitoring basic parameters such as pH, soil moisture, or temperature are commonly available on the market. However, if farmers are to face current challenges, including climate change, and ensure sufficient food for humanity, they need much more effective tools that will enable them to monitor, for example, various pathogens, including bacteria and fungi. In our opinion, a suitable solution is a combination of new smart materials and printing for the production of inexpensive, durable, and scalable materials,” said the article’s first author, David Panáček from CATRIN, who worked on the study during his internship at Imperial College London.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CATRIN_Soucasne_senzory_nestaci_Vedci_navrhuji_novou_cestu_ke_sledovani_zdravi_rostlin_b4014952a3.jpg" alt="CATRIN: David Panáček" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CATRIN_Soucasne_senzory_nestaci_Vedci_navrhuji_novou_cestu_ke_sledovani_zdravi_rostlin_b4014952a3.jpg 208w," sizes="100vw" width="1536" height="1152">Sensors for monitoring plant health, for example, lag behind similar devices used in human medicine. According to the authors, advances in materials science, which will enable the development of scalable sensor technologies, play a key role in this potential shift. “Printing techniques, including inkjet printing, screen printing, aerosol printing, 3D printing, and direct laser writing, offer flexible ways to produce flexible sensors, large-area sensors, and sensors integrated directly into plants. The review article summarizes recent advances in printable low-dimensional materials for agricultural sensors, analyzes their physico-chemical properties in relation to sensor performance, and discusses key challenges and future opportunities requiring interdisciplinary integration,” said one of the corresponding authors, Michal Otyepka.The research brought together materials scientists, chemists, biologists, sensing experts, and printing technology specialists. Materials research and the use of graphene-based smart materials were led by scientists from CATRIN at Palacký University and VŠB-Technical University of Ostrava. Plant biologists from CATRIN contributed their knowledge of plant development, their responses to stress conditions, and the monitoring of their properties. Researchers from Imperial College London took care of the electronics, while representatives from<a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/companies/36"> CEITEC – VUT</a> focused on printing technologies. The team also included leading experts in sensing from the Catalan Institute of Nanoscience and Nanotechnology in Barcelona, and Joseph Wang of the University of California San Diego, the “father of sensing and electrochemistry,” also contributed his extensive knowledge.“This is a groundbreaking study on this topic, which has managed to attract some truly big names in their respective fields. Last but not least, the study demonstrates that interdisciplinarity at CATRIN gives rise to completely new and promising research topics, such as plant sensing and its use for studying plant-environment interactions and smart agriculture,” added another corresponding author, Nuria De Diego.

Current sensors are not good enough. Scientists propose a new way to monitor plant health

In this episode of the Concentrating on Chromatography podcast, host David Oliva interviews Ainslie Chen about her cutting-edge research on hemoglobin variant testing using liquid chromatography-high resolution mass spectrometry (LC-HR-MS). Ainslie discusses her novel method for separating and identifying hemoglobin subunits with mass shifts less than 1 Da, overcoming critical limitations in conventional clinical assays.Hear firsthand how her team developed an LC-HR-MS workflow using a C4 reversed-phase column, tackled technical challenges (including why C18 columns fell short), and achieved unprecedented sensitivity for variant detection in both adult and neonatal samples. The conversation touches on the potential of mass spectrometry to revolutionize clinical diagnostics, the importance of reproducibility, barriers to adoption in routine labs, and how teamwork drives scientific innovation.Perfect for analytical chemists, clinical laboratorians, and anyone interested in the future of protein variant analysis, this episode also features Ainslie’s advice for early-career scientists and insights from her first ACS poster presentation.<h4>Key Highlights:</h4><ul><li>Motivation behind improving hemoglobinopathy testing &nbsp;</li><li>Technical advantages of LC-HR-MS over gene sequencing and CE &nbsp;</li><li>The crucial role of the C4 column in resolving challenging samples &nbsp;</li><li>Critical parameters for reproducible LC-HR-MS workflows &nbsp;</li><li>Barriers and outlook for clinical adoption of advanced mass spectrometry &nbsp;</li><li>The value of teamwork and mentorship in scientific research &nbsp;</li><li>Direct insights from recent ACS conference experiences</li></ul><h3>Video transcription</h3>In this interview, Ainslie Chen discusses her research on improving the detection and identification of hemoglobin variants using liquid chromatography coupled with high-resolution mass spectrometry (LC-HRMS). The work addresses limitations of conventional hemoglobinopathy testing, which often struggles to resolve very small mass differences between closely related hemoglobin subunits. Because even a single amino-acid substitution can significantly alter hemoglobin structure and function, high analytical resolution is essential for accurate diagnosis of conditions such as anemia and sickle cell disease.Chen explains why her team selected LC-HRMS over established clinical techniques like capillary electrophoresis and gene sequencing. While sequencing offers excellent accuracy, it is time-consuming, costly, and requires extensive sample preparation, making it impractical for routine clinical workflows. Capillary electrophoresis enables subunit separation but lacks the resolving power needed to distinguish variants differing by less than one Dalton. In contrast, high-resolution mass spectrometry provides both structural specificity and sensitivity, enabling confident identification of subtle hemoglobin variants with minimal sample preparation.A key methodological insight from the project was the use of a C4 reversed-phase LC column instead of the more common C18 column. Chen describes how the shorter carbon chain and larger pore size of C4 columns improved protein elution and reduced denaturation, leading to more reproducible separations. Critical parameters for reproducibility included consistent mobile-phase composition (0.1% formic acid in water and acetonitrile), controlled temperature (60 °C for LC, ~320 °C capillary temperature), and stable chromatographic conditions.Beyond hemoglobin analysis, Chen highlights the broader potential of high-resolution mass spectrometry in proteoform analysis and clinical diagnostics, including emerging applications in cancer detection. She acknowledges current barriers to clinical adoption—such as energy demands and instrument infrastructure—but points to advances like miniaturized mass spectrometers as promising steps toward wider use. The interview concludes with advice for young scientists: don’t hesitate to reach out to mentors, embrace collaboration, and view analytical chemistry as a versatile tool that bridges medicine, biology, environmental science, and beyond.<blockquote>This text has been automatically transcribed from a video presentation using AI technology. It may contain inaccuracies and is not guaranteed to be 100% correct.</blockquote><blockquote><h4>Concentrating on Chromatography Podcast</h4>Dive into the frontiers of chromatography, mass spectrometry, and sample preparation with host David Oliva. Each episode features candid conversations with leading researchers, industry innovators, and passionate scientists who are shaping the future of analytical chemistry. From decoding PFAS detection challenges to exploring the latest in AI-assisted liquid chromatography, this show uncovers practical workflows, sustainability breakthroughs, and the real-world impact of separation science. Whether you’re a chromatographer, lab professional, or researcher you'll discover inspiring content!You can find Concentrating on Chromatography Podcast in podcast apps:<ul><li><a target="_blank" rel="noopener noreferrer" href="https://open.spotify.com/show/1wZg67rCjoGju4yhqxI3tL">Spotify</a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podcasts.apple.com/tz/podcast/concentrating-on-chromatography/id1788429185">Apple podcast</a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podscan.fm/podcasts/concentrating-on-chromatography">podscan</a></li></ul>and on <a target="_blank" rel="noopener noreferrer" href="https://www.youtube.com/@ChromatographyTalk/videos">YouTube channel</a></blockquote>

Unlocking Hemoglobin Variant Detection: LC-HR-MS Breakthrough with Ainslie Chen

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The Czech Advanced Technology and Research Institute (CATRIN) at Palacký University is a cutting-edge scientific hub dedicated to advancing research in the fields of nanotechnology, biotechnology, and biomedicine. At its core, CATRIN boasts outstanding scientific teams, featuring international researchers. We emphasize interdisciplinarity, foster global collaborations, and work to translate our research findings into practical applications.

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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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Identification of the substance – what is in your sample? (Bioanalytic)

We are able to identify metabolites and products of chemical reactions, contaminants of biological and chemical substances and preparations, and perform profiling of a series of samples to study the kinetics of transformations.

<h4>Substance Identification - Looking for answers to what's in your sample? - we can help you.</h4>Substance identification based on LC-MS/MS techniques can involve single compounds or mixtures of substances. In our analyses, we rely primarily on the knowledge and skills we have acquired after many years of work. For analysis, we use full laboratory facilities for sample preparation and high-resolution mass spectrometry (<a target="_blank" rel="noopener noreferrer" href="https://labexperts.com.pl/o-nas/">equipment</a>).We use different work algorithms depending on the material we are dealing with and the analytical task to be solved. We use DDA (IDA) or DIA (SWATH) methods or targeted approaches (e.g. MRMhr) if we know what to expect. Thus, we are able to identify metabolites and products of chemical reactions, contaminants of biological and chemical substances and preparations, and perform profiling of a series of samples to study the kinetics of transformations.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Identification_of_the_substance_what_is_in_your_sample_2_0f425a648b.jpg" alt="Bioanalytic: Identification of the substance – what is in your sample" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Identification_of_the_substance_what_is_in_your_sample_2_0f425a648b.jpg 245w," sizes="100vw" width="1881" height="1156"><h4>COST OF SERVICE</h4>We determine the cost of the service individually. The final cost is influenced by many factors related to the nature of the sample itself and the client's expectations. Thus, the price depends, among other things, on the complexity of the sample preparation procedure, the scope and number of analyses, etc.The service includes (depending on individual arrangements):<h5>Development of sample preparation procedure</h5><ul><li>Depending on the matrix and test substances.</li></ul><h5>Development of analytical methods</h5><ul><li>Application of high-resolution LC-MS/MS analyses using DDA (IDA) or DIA (SWATH) experiments and software to support the development of targeted screening methods.</li></ul><h5>Analysis of results includes:</h5><ul><li>finding and identifying the substances of interest, interpreting MS/MS spectra and proposing a structural formula.</li><li>Comparative analysis of sample series, e.g. PCA,</li><li>profiling of analytes in sample series</li></ul><h5>Reporting of results</h5><ul><li>Compile results into easy-to-read reports.</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Identification_of_the_substance_what_is_in_your_sample_3_c1b8adc1d0.jpg" alt="Bioanalytic: Identification of the substance – what is in your sample" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Identification_of_the_substance_what_is_in_your_sample_3_c1b8adc1d0.jpg 245w," sizes="100vw" width="1919" height="1208">

Characteristics of monoclonal antibodies (Bioanalytic)

At LabExperts, proteomic analyses are performed on a ZenoTOF 7600 high-resolution LC-MS/MS system (SCIEX). For MS/MS analyses, we use Collision induced dissociation (CID) and Electron-Activated Dissociation (EAD) fragmentation.

Antibodies are molecules made up of 4 polypeptide chains: two heavy (H - high-chain) linked to each other by a specific type of chemical bond - a disulfide bridge, and two light (L - light-chain) linked by an identical bond to the heavy chains. Monoclonal antibodies (mABs) are used in various forms - as free molecules, in the form of a drug-antibody combination, and in the form of an immunoconjugate, a drug-antibody-biopolymer combination.Their main use is in highly specific targeted therapy for cancer, cardiovascular, autoimmune and nervous system diseases. They are also used in the treatment of osteoporosis, Alzheimer's disease or transplantation. The range of applications of monoclonal antibodies is systematically expanded. The introduction of a new antibody to the market requires complex product characterization, which involves numerous proteomic analyses, which are performed by LC-MS/MS techniques, among others.<h4>LC-MS/MS</h4>The characterization of monoclonal antibodies involves many aspects, including, but not limited to, a suite of analyses related to confirmation of the structure, chain sequence and degree of modification of the antibody. Post-translational modifications (PTMs) are chemical changes that occur after the translation process. These changes generally result in an increase in the immunogenicity of the drug. For this reason, it is essential to monitor modifications as critical quality attributes (CQAs) during both the production and storage of the drug. To ensure monitoring of CQA points, the primary structure of the protein is characterized based on peptide mapping (peptide mapping) analysis. The protein under study is subjected to proteolytic digestion using enzymes such as trypsin, chymotrypsin, Lys-C, Glu-C. As a result of various proteolytic enzymes, a wide range of peptides is obtained. Ultimately, coverage of the entire sequence of the protein under study is obtained.<figure class="image"><img style="aspect-ratio:1536/947;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_3_d94fa1623b.jpg" alt="Bioanalytic: Characteristics of monoclonal antibodies." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_3_d94fa1623b.jpg 245w," sizes="100vw" width="1536" height="947"></figure>At LabExperts, proteomic analyses are performed on a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=52&amp;search=ZenoTOF+7600">ZenoTOF 7600</a> high-resolution LC-MS/MS system (SCIEX). For MS/MS analyses, we use Collision induced dissociation (CID) and Electron-Activated Dissociation (EAD) fragmentation. This provides us with data for unambiguous identification of protein-building amino acids. We process the results using Sciex OS, Skyline and Spectronaut software.<blockquote>We perform:<ul><li>Whole protein analyses - Intact - to determine the exact mass and confirm the theoretical mass;</li><li>N-glycosylation profile determination (based on MS spectrum reconstruction):<ul><li>Glycosylated form;</li><li>Deglycosylated;</li><li>Glycosylated with reduced disulfide bridges;</li><li>Deglycosylated with reduced disulfide bridges.</li></ul></li><li>Peptide maps:<ul><li>Protein digestion with various proteases so that sequence coverage is close to 100%<ul><li>Analysis of PTMs:</li><li>Location of modifications</li></ul></li><li>[%] of modifications compared to the unmodified sequence</li></ul></li><li>TiPOS testing - (technical proof of similarity) - technical confirmation of the similarity of the protein synthesized by the customer (from several LOTs) with the target protein (provided as a template).</li></ul>In order to maintain the highest possible analytical standards, we perform monoclonal antibody analyses under the regime of an internally developed and implemented laboratory quality system based on GLP principles.See also our other proteomics services: <a target="_blank" rel="noopener noreferrer" href="https://labexperts.com.pl/service/identyfikacja-bialek/">Protein identification</a>, <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1294">Protein quantitative analysis</a></blockquote><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_2_cb93143fe6.jpg" alt="Bioanalytic: Bioanalytic Characteristics of monoclonal antibodies." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_2_cb93143fe6.jpg 245w," sizes="100vw" width="1536" height="908"><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_1_0e8ab7cdfa.jpg" alt="Bioanalytic: Bioanalytic Characteristics of monoclonal antibodies." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_1_0e8ab7cdfa.jpg 245w," sizes="100vw" width="1536" height="858">

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">

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