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

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

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

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

Why Biologics QC Is So Much Harder Than Small Molecule Pharma

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

Czech Academy of Sciences

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

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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><strong>Substance Identification - Looking for answers to what's in your sample? - we can help you.</strong></h4><p>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>).</p><p>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.</p><p><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"></p><h4><strong>COST OF SERVICE</strong></h4><p>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.</p><p><strong>The service includes (depending on individual arrangements):</strong></p><h5><strong>Development of sample preparation procedure</strong></h5><ul><li>Depending on the matrix and test substances.</li></ul><h5><strong>Development of analytical methods</strong></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><strong>Analysis of results includes:</strong></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><strong>Reporting of results</strong></h5><ul><li>Compile results into easy-to-read reports.</li></ul><p><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"></p>

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.

<p><strong>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.</strong></p><p>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.</p><h4><strong>LC-MS/MS</strong></h4><p>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.</p><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><p>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"><strong>ZenoTOF 7600</strong></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.</p><blockquote><p><span style="font-size:22px;"><strong>We perform:</strong></span></p><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><p>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.</p><p>See also our other proteomics services: <a target="_blank" rel="noopener noreferrer" href="https://labexperts.com.pl/service/identyfikacja-bialek/"><strong>Protein identification</strong></a>, <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1294"><strong>Protein quantitative analysis</strong></a></p></blockquote><p><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"></p><p><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"></p>

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.

<p><strong>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.</strong></p><p><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"></p><h4><strong>LC-MS/MS</strong></h4><p>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 <i>collision induced dissociation</i>(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"><strong>ZenoTOF 7600</strong></a> (SCIEX), in which the Zeno ion trap and EAD (<i>Electron-Activated Dissociation</i>) 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.</p><blockquote><p><span style="font-size:22px;"><strong>We perform analyses of:</strong></span></p><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><p>Qualitative analysis of proteins includes:</p><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><p><span style="font-size:22px;"><strong>Comparative analyses include:</strong></span></p><ul><li>Determining the composition of mixtures;</li><li>Comparison and profiling of sample series - protein identification and trend analysis.</li></ul><p><span style="font-size:22px;"><strong>Our offer also includes</strong>:</span></p><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"><strong>Quantitative analysis of proteins</strong></a>;</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1296"><strong>Analysis and characterization of monoclonal antibodies</strong></a>.</li></ul></blockquote><p><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"></p>

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Why Biologics QC Is So Much Harder Than Small Molecule Pharma

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

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