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State Key Laboratory of Elemental Organic Chemistry, Nankai University | |||
 | Associate Dean, School of Chemistry, Nankai University Director, Department of Chemical Biology, Nankai University Xi Zhen Research direction: protein-protein Http://skleoc.nankai.edu.cn/professors/xiz/index.html | ||
Our recent research is focused on the molecular basis of herbicide resistance and exploiting new target sites of herbicide, such as PPI of AHAS. Via MST, we measured the Protein-Protein interaction, that have been difficult to detect and quantify with ITC because of unstable Of the protein and very little heat changes of our samples. The MST technology can be used as a complementary technology to the traditional methods in these fields. We can strongly recommend the MST technology for its low material consumption, short measurement times and broad application range in the field of molecule interaction studies. We are currently working on the molecular mechanisms of herbicide resistance and the search for new herbicide targets (such as the interface between AHAS subunits). Through MST , we measured protein - protein interactions, and our samples were not determined using the ITC method because our samples were less stable and the interaction heat was minimal. So in these areas of research, MST technology is well complemented by traditional technologies. We highly recommend some of the features of MST technology, such as low sample usage, short measurement times, and a wide range of applications for intermolecular interactions . | |||
Institute of Biophysics | |||
 | Director of the Center for Molecular Biology, Institute of Biophysics, Academician of the Chinese Academy of Sciences Wang Dacheng Research direction: Protein - DNA Http://sourcedb.cas.cn/sourcedb_ibp_cas/ | ||
Our resent research is focused on the critical pathogenic protein & complex from pathogenic microbes and The Protein structure-functional basis for some endogenous disease. Via MST, we measured the Protein-DNA interaction, that have been difficult to detect and quantify with other standard biomolecule interaction technologies (like SPR and ITC) because of the conformation/immobilization-sensitive and very little heat changes of our samples. MST technology Can be used as a complementary technology to the traditional methods in these fields. We can strongly recommend MST technology for its low material consumption, short measurement times and broad application range for molecule-interaction studies. We are currently working on the structure-function and molecular mechanisms of important pathogenic pathogenic proteins and the protein structure-functional basis of some endogenous diseases. Through MST, we measured protein-DNA interactions, and our samples were difficult to measure by other traditional methods (such as SPR and ITC ) because our sample conformation is sensitive to fixation and has minimal heat changes. So in these areas of research, MST technology is well complemented by traditional technologies. We highly recommend some of the features of MST technology, such as low sample usage, short measurement times, and a wide range of applications for intermolecular interactions . | |||
School of Life Sciences, Shandong University | |||
 | Doctoral tutor of the International Key Laboratory of Microbial Technology, Shandong University 985 platform academic leader Gu Lichuan Research interests: protein- small molecule inhibitors, protein structure and function Http:// | ||
Part of our research focus on the protein structural-function basis for iron metabolism of pathogenic microorganisms. We measured the dissociated constant for periplasmic binding protein and siderophore through MST technology. Because siderophore is extremely insoluble, it's difficult for us to complete that task via other Methods such as ITC and SPR. We strongly recommend MST technology for its low material consumption, short measurement time and very wide application range. (Editor's translation) Some of our current topics are about the structure and function of proteins involved in iron metabolism of pathogenic microorganisms. Through MST technology, we measured the dissociation constants of periplasmic space transferrin and iron carriers. Our samples are difficult to measure by other traditional methods (such as SPR and ITC) because of the extremely low solubility of small molecules, we are using MST technology. The ideal result was obtained. We highly recommend some of the features of MST technology, such as extremely low sample usage, faster measurement times, and a wide range of applications . | |||
French Sanofi company R & D department | |||
 | User: Dr. Alexey Rak Research direction: drug development | ||
"We routinely assess interaction affinity for both small molecule and biologics projects, with NanoTemper Technologies' Microscale Thermophoresis being the most recent addition to the pool of instruments we use to carry out these measurements. It has proved a valuable tool for characterising small molecule-protein And protein-protein interactions, as well as for the study of protein aggregation concentration determination. There is very good agreement with other technologies such as Surface Plasmon Resonance (SPR) and Isothermal Titration Calorimetry (ITC), and we are particularly appreciative of this new Technology because of the extremely low protein consumption and relatively short time required for the assay setup. NanoTemper customer support has been a key factor in enabling us to familiarise ourselves with the new technology. We would like to deploy increased numbers of applications based on MST technologies And continue to interact with NanoTemper Technologies Company, a dyna Mic, scientifically driven company." (Editor's translation) We often need to measure the interaction affinities of small molecules and biologics. The latest device we have recently used is NanoTemper's micro-thermal mobility technology. The results demonstrate that MST is a valuable tool for measuring small molecule-protein, protein interactions, and determining the concentration of protein-forming aggregates. MST technology is in complete agreement with other traditional techniques such as surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC). We particularly like the features of this new technology: very low protein sample usage and very short experiments. Set the time . NanoTemper's technical support is very timely and efficient, allowing us to quickly become familiar with this new technology. We are willing to use more and more MST instruments and continue to work with NanoTemper Technologies because of this positive, technologically advanced company. | |||
Institute of Medicinal Chemistry, Phillips University, Marlborough, Germany | |||
 | Website: http:// User: Prof. Gerhard Klebe Research direction: Structural drug design | ||
The main focus of our work lies on structure based-drug design. In this context, we study the interaction of the bacterial tRNA modifying enzyme tRNA-guanine transglycosylase (Tgt) with small molecule inhibitors and with tRNA. interaction of this enzyme with its small molecule substrates guanine and 7-deaza-7-aminomethyl guanine via MST, a strong influence on the thermophoretic behaviour of Tgt was noticed upon binding of the Macromolecular tRNA substrate allowing determination of the respective Kd value. In addition , MST yielded Kd values ​​for lin-benzoguanine-based Tgt inhibitors (300-500 Da), which were excellently consistent with Ki values ​​previously determined in enzyme kinetic studies. subsequent, this fast and easy to use method provides a highly welcome alternative to the Radioactive enzyme assay we used so far to figure out binding affinities of Tgt inhibitors. further, we investigate the interaction of a chaperone of the Shigella typ e III secretion system with its protein interaction partners or rather with synthetic peptides thereof to identify the respective recognition motifs. Via MST, we determined with low amounts of protein material Kd values ​​which were in nearly perfect agreement with those measured via isothermal titration calorimetry. (Editor's translation) Our main job is to design drugs based on structure. For example, the interaction of bacterial tRNA-modifying enzyme-tRNA guanine transglycosidase (Tgt) with small molecule inhibitors and tRNA. Although we cannot directly measure the interaction of this enzyme with small molecule guanine and 7-deaza-7-aminomethyl, since Tgt binds to macromolecular tRNA with obvious thermodynamic changes, we can measure each by MST. Kd value. In addition, the Kd values ​​of lin-benzoguanine-based MST Tgt inhibitors (300 - 500 Da) measured by MST were excellently consistent with the Ki values previously determined by enzyme kinetic studies . Therefore, this fast and easy-to-use method provides a very good method for replacing radioactive enzyme activity assays, which is a method we have previously used to measure the affinity of Tgt inhibitors. We used to find binding affinity Tgt inhibitors so far. In addition, we also studied the interaction of a Shigella type III secretion system chaperone protein with its conjugate (synthetic peptide). Through MST, we can measure Kd values ​​with very low amounts of protein , and the results are almost in perfect accordance with the data obtained by traditional isothermal titration calorimetry ITC and other technologies . | |||
French National Research Center | |||
 | Http://seg.ihes.fr/ User: Dr. Arndt Benecke Research direction: small non-coding RNA | ||
We use systems biology to study transcription regulatory phenomena on a genome-wide scale in the context of host-pathogen interactions and cancer. Microscale Thermophoresis (MST) has had extremely useful to rapidly quantify relevant protein-nucleic acid and protein-protein interactions directly in cellular lysates without going through the hassles of purification. (Editor's translation) We use systematic biology methods to study transcriptional regulation in a genome-wide manner, targeting cancer and host-pathogens. The Micro Thermophoresis (MST) method is a valuable method because it rapidly quantifies the interaction between protein - nucleic acids and proteins, and does not require complex and cumbersome purification to perform measurements in cell lysates . | |||
American Anderson Cancer Center | |||
 | http://faculty.mdanderson.org/John_Ladbury User: Prof. John E. Ladbury Research direction: tyrosine kinase-mediated signal transduction | ||
In my group we explore the structural, biophysical, and cellular outcomes of protein complex formation at membrane-bound receptors. We use Microscale Thermophoresis (MST) in addition to other methods including isothermal titration calorimetry and surface plasmon resonance and find a good agreement between the methods. We are very pleased with the Low material consumption, short measurement times and broad application range of MST . (Editor's translation) In my research group, we explore structural, biophysical and membrane-bound receptor protein complexes. We used a micro-thermal kinetic spectrometer ( MST ) to find that the technique is in good agreement with other traditional techniques for isothermal titration calorimetry ITC and surface plasmon resonance SPR , and the sample consumption of MST is extremely low. The time is short and the range of applications is wide. | |||
Free University of Brussels, Belgium | |||
| http:// User: Prof. Han Remaut Research Interests: Structural Molecular Biology of Bacterial Cell Surfaces | ||
We study the structural and molecular biology of bacterial adhesins and cell-surface filaments with respect to their function in bacterial pathogenesis, with the ultimate aim of developing a new generation of virulence-targeted antimicrobials. MST really is opening up the easy determination of some Kd's that were hard to get to with other methods. So far, we measured protein-protein, protein-glycan, protein-small compound and protein-cofactor interactions with the Monolith NT.115. †(Editor's translation) We studied the structural and molecular biological properties of bacterial adhes and cell surface filaments to illustrate the pathogenesis of bacteria, with the ultimate goal of developing a new generation of targeted antibiotics. MST is really a very easy way to measure Kd values, and many Kd values ​​are difficult to accomplish using other traditional methods. So far, we have measured the interaction of protein-protein, protein-polysaccharide, protein-small compound and protein-coenzyme factor using the labeled MST-NT.115. | |||
University of Cincinnati School of Medicine | |||
 | User: Yi Zheng, PhD Research direction: Signal transduction – Rho GTPases | ||
We are studying the molecular mechanisms of signal transduction processes involving Rho GTPases and are developing small molecule inhibitors and other strategies that interfere with specific Rho protein functions in leukemia, lymphoma and lung cancer. We are very enthusiastic about MST as it quickly enabled us to measure protein:protein and protein:small molecule interactions that have been difficult to detect and quantify with standard biomolecule interaction technologies in the past years. MST provides us with a unique tool to validate the Lead inhibitors that bind to specific sites of Rho GTPases or their regulators/effectors . (Editor's translation) We are investigating the molecular mechanisms of signal transduction of Rho GTPases and developing small molecule inhibitors and other methods for specifically interfering with Rho protein function in leukemia, lymphoma, and lung cancer. We like MST technology very much , because in the past few years MST has helped us to quickly measure the interaction between protein - protein and protein - small molecules, and it is often difficult to use other standard biomolecular interaction techniques. MST provides us with a unique tool to verify whether an important inhibitor binds to a specific site of Rho GTPases or binds to its modulator/effector. | |||
Max-von-Pettenkofer Institute, University of Munich, Germany | |||
| User: Dr. Maria G. Vizoso Pinto Research direction: viral infection | ||
"Our lab is developing diagnostic tools based on protein biochips and is studying the basic mechanisms underlying herpes virus infections" We are using MST for elucidating the function of viral proteins and its interaction with other viral and host cell proteins. MST is simple to use and was quickly established in our lab. In particular we do appreciate the low instrument, consumables and maintenance costs associated with this new technology †(Editor's translation) Our laboratory is developing a biochip-based diagnostic tool that is the basic mechanism for studying herpes virus infection. We use MST to elucidate the function of viral proteins and their interaction with other viral and host cell proteins. MST is easy to use and will soon be available in our labs. We especially appreciate the low cost and maintenance costs of new technologies and responsive instruments. | |||
Aarhus University, Denmark | |||
| Http:// User: Prof. Jens Stougaard Research direction: the function of polysaccharides | ||
We are interested in understanding the interactions between cells and organisms by investigating the role of polysaccharides exposed on cell surfaces and secreted polysaccharide signal molecules. We are applying MST to determine structural requirements for recognition of complex polysaccharides and the role of ligand-receptor interactions in The relationships between different cells and organisms. MST is very useful for my lab since it allows to measure interactions in solution even in complex samples of membrane proteins. Also the small amount of sample material needed and the broad range of applications are very advantages." (Editor's translation) Our laboratory reveals the interaction of cells with cells and organisms by studying the polysaccharides and secreted polysaccharide signaling molecules exposed on the cell surface. We use MST to measure complex polysaccharide binding and ligand-receptor binding to elucidate interactions between different cells or organisms. MST is very useful in our laboratory because it measures the interaction of membrane proteins in complex environmental solutions. In addition, only a small amount of sample consumption and a wide range of applications are also the advantages of MST . | |||
Free University of Berlin, Germany | |||
| Http:// User : Prof. Dr. Joachim Heberle Research direction : Structure and function of membrane proteins | ||
My topic focuses on the elucidation of the structure and function of membrane proteins. We are employing MST in binding studies of membrane sensors to their transducers as well as soluble transcription factors to DNA. We also plan for investigations of receptor - ligand interactions with this exciting new technique. MST turned out to be an extremely useful method in our lab to determine binding constants. It is beneficial that the fast and handy. (Editor's translation) Our laboratory specializes in the study of the structure and function of membrane proteins, including protein-protein and protein-substrate interactions. We used MST to study the binding reaction of membrane protein sensor molecule - sensor molecule - transcription factor -DNA . MST shows excellent advantages, including fast and simple measurements, low sample consumption, and more. | |||
University of Regensburg, Germany | |||
| User : Prof. Dr. Gernot Längst Research direction: Chromatin dynamics and nuclear assembly | ||
Our lab focuses on the mechanisms and organization of DNA packaging inside the cell nucleus. We study the biochemical properties of molecular machines, the chromatin remodelers that regulate DNA accessibility and switch between 'on' and 'off' states of genes. We are using MST for studying the activity of chromatin remodeling enzymes and to quantify their affinities towards DNA, RNA and other proteins. MST is a good alternative to the traditional electrophoretic mobility shift assays. MST is simple to use and was quickly established in our lab. (Editor's translation) Our laboratory specializes in studying the mechanisms of DNA packaging in cells and among them, studying the biochemical properties of molecular machines, and chromatin remodeling regulates DNA assembly and regulates the switching state of genes. We studied chromatin recombinases by MST and quantified their affinity for DNA, RNA and other proteins. MST takes quantitative biochemical technology to a new level because it is easy to learn and replaces traditional EMSA technology very well. | |||
Munich University, Germany | |||
| User : Prof. Dr. Axel Imhof Research direction: experimental embryology - histone coding | ||
We are interested in the basic mechanisms in epigenetics which define and maintain the histone code and are using MST to measure the binding of "reader"-proteins to modified histone peptides as well as the activity and inhibition of "writer" enzymes including kinases, demethylases And methylases. The new MST technology is easy to use and a good alternative to our standard enzymatic assays which are radioactive and measure endpoints only. It allows us to easily measure affinities for protein-peptide interactions in solution. (Editor's translation) We are interested in the definition of experimental embryology and the basic mechanisms for maintaining histone guidelines, and use MST to measure the binding of "Reader" proteins to modified histone polypeptides and "writer" enzymes (including kinases, demethylation). Activator and inhibitor of enzyme, methylase). The latest MST technology is very easy to learn and is an excellent replacement technique for traditional methods such as radioactive terminal measurement, and MST is the affinity for measuring protein - protein interactions in solution . | |||
University of Frankfurt, Germany | |||
User : Prof. Dr. med. Liliana Schaefer Research direction : Matrix signaling pathways in inflammation and fibrosis | |||
The work of our group gave rise to the novel concept that under certain conditions matrix components may act as endogenous "danger" signals, which are recognized by innate immunity receptors, and are capable to trigger an inflammatory response reaction. The affinities are consistent with the biological readouts and confirm previous results gained with immunprecipitation and binding Assays. MST is a new technology we can definitely recommend for obtaining robust quantitative affinity data." (Editor's translation) We have found that certain matrix components become endogenous "dangerous" signals in specific wells, and these abnormal components are recognized by innate immune receptors and can trigger an inflammatory response. We used MST to measure the endogenous/in vivo mutant proteoglycans in the extracellular matrix and their related receptor responses, and were very satisfied with all the data currently available, and the data obtained were completely consistent with those predicted by other biological methods. Data previously obtained using immunoprecipitation and binding assays were validated. MST is a very new technology and we recommend this technique to get very good quantitative affinity data. | |||
University of Munich, Gene Center | |||
| User : Prof. Dr. Klaus Förstemann Research direction: The biological origin of miRNAs in Drosophila | ||
We are studying the processing of microRNA precursors In Drosophila and are using MST to measure the binding of nucleolytic Enzymes and their specificity factors to RNA substrates. The small amount of protein sample needed and the much faster measuring time compared with eg gel-shift assays are particular strengths of this new technique. It enables us to ask questions that we could not address before. (Editor's translation) We are studying the microRNA development process of Drosophila precursor cells and using MST to measure the binding of a ribozyme, a specific factor, to RNA. MST's minimal protein sample consumption and extremely short measurement times make him a very valuable technology that can help us answer many questions that were previously unexplained. | |||
Department of Physical Chemistry, Gothenburg University, Germany | |||
| User : Prof. Dr. Andreas Janshoff Research direction : the role of membrane vesicles | ||
Membrane interaction and fusion plays a fundamental role in many cellular processes such as intracellular trafficking, fertilization, tissue formation or viral infection. With the new MST technology we were able to measure the interaction of membrane vesicles, mediated by coiled coil-forming peptides. The technology requires only little sample material and is enabling for this type of experiments†The fusion of biofilms plays a very important role in the interaction of multiple processes in the cell (intracellular transport, fertilization, tissue formation, and viral infection). Through MST technology, we were able to measure helical polypeptide-mediated vesicle interactions. This technology requires very little sample material to complete the measurement. | |||
Institute of Organic Chemistry and Biomolecular Sciences, Gothenburg University, Germany | |||
| User: Prof. Dr. Ulf Diederichsen Research direction : synthetic biomolecules | ||
We are interested in the biophysical properties of soluble and membrane bound biomolecules and are using MST to measure binding affinities and complex formation. MST is straightforward and fits well in our technology portfolio to cover a broad spectrum of synthetic biomolecules including proteins, peptides and nucleic acids. (Editor's translation) The fusion of biofilms plays a very important role in the interaction of multiple processes in the cell (intracellular transport, fertilization, tissue formation, and viral infection). Through MST technology, we were able to measure helical polypeptide-mediated vesicle interactions. This technology requires very little sample material to complete the measurement. We are interested in the biophysical properties of free and on-membrane biomolecules and use MST to measure binding affinity and conformation of the complex. MST technology is simple to use and well integrated into our current technology system, enabling us to study a wide range of synthetic biomolecules, including proteins, peptides and nucleic acids. | |||
Massachusetts Institute of Technology | |||
 | Http://web.mit.edu/lms/www/ User : Dr. Shuguang Zhang Professor Zhang Shuguang Research direction : molecular structure | ||
We are interested in molecular architectures especially to stabilize and analyze challenging smells that belong to G protein-coupled receptors (GPCRs). GPCR is a super-family of receptors linked to many diseases. We want to measure the interactions of smell receptors with odorant In the past that has been extremely difficult to detect and quantify other common molecular interaction technologies including SPR, and nearly impossible to use ITC for odorant-binding measurement because of the conformation and immobilization-sensitivities, or difficult And costly to obtain sufficient amount of receptors. The MST technology is a superb technology, it not only is label-free, hence reducing the measuring artifacts, but it also is surface-free that provides true measurement of finest molecular interactions. Us much better analysis of the GPCR with their small-molecule ligands. We strongly recommend MST technology for its low mat Erial consumption (a few micrograms in a few microliters), short measurement times, inexpensive consumables, and broad application range in all molecule-interaction study. Our research direction is molecular structure, especially the stability and analysis of olfactory receptor molecules associated with G-protein coupled receptors (GPCRs). GPCRs are a superfamily of receptors associated with many diseases. We want to measure the interaction between the olfactory receptor and the fragrance molecule, and the fragrance molecules are usually very low molecular weight ligands. In the past, methods of other intermolecular interactions (including SPR) have been difficult to detect and quantify due to the conformational correlation and immobilization sensitivity of the fragrance binding reaction , and a small amount of fragrance can be obtained due to the need for expensive and difficult methods. Agent molecules are also impossible through ITC technology. MST technology is a very good method. It can analyze the artificial artifacts in the experiment without labeling, and it does not need to be fixed. It can provide real data of intermolecular interactions, so it can make us better analyze GPCR and small. The role of molecular ligands. We strongly recommend several features of MST technology: extremely low sample consumption (several micrograms / microliters) , short measurement time, inexpensive consumables, and a wide range of applications in molecular interaction studies. | |||
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