"One mission of the Structural Research group within the Lead Identification and Optimization department is to quantitatively validate and characterize interactions of small molecules as well as new biological entities with protein targets. We employ various traditional biophysical methods such as SPR, Thermal Shift, ITC, NMR and X-ray crystallography. 
Most recently we included Microscale Thermophoresis (MST) in our standard project support workflow and extended its application from affinity determinations to fragment screening approaches. MST is a versatile and valuable tool which we quickly adapted in our repertoire of methods. The impressive advantages of MST, namely the low sample consumption, the broad application range, and swift assay development make it a unique biophysical method. The measurement in free solution without the need of surface coupling saves time and avoids a potential source for false positive or negative results. 
Our Structural Research group now also added the label-free version of the Monolith to our MST instrumentation portfolio, which gives us the possibility to choose to measure with high selectivity and sensitivity (NT.115). The labelfree version (NT.LabelFree) allows us to measusre without any additional sample modification depending on the need of the particular assay. In some cases, LabelFree MST allowed us to perform assays with otherwise "very ill" behaved proteins which were not amenable to any other biophysical technique. Generally, we find very good consistency between quantitative MST measurements and results stemming from other biophysical methods."

Dr. Markus Zeeb, Principal Scientist, Structural Research, Boehringer-Ingelheim, Germany

"As part of our drug discovery projects we use Microscale Thermophoresis (MST) as an orthogonal method to measure the binding affinity of compounds to their protein target and apply this fragment hit ID through to lead optimisation. MST complements our biophysical platform and has correlated well with other more established technologies. Because it uses small amounts of protein, MST has proved to be particularly useful to look at molecular interaction involving proteins that are difficult to express or purify. MST requires a relatively short time to setup new assays and is a powerful technique for buffer optimisation. Using the NT.115 MST instrument we have successfully measured small molecule-protein and protein-protein interactions in complex media. Finally, LabelFree MST is one of the few true label-free/immobilisation-free instruments capable of measuring molecular interactions. We have appreciated the professionalism and support from NanoTemper Technologies."

Dr. Nicolas Basse, Department of Structural Biology, UCB-Celltech, UK

http://www.ucbpharma.co.uk/home

A few years ago, we were seeking for a biophysical method orthogonal to ITC and SPR. With MicroScale Thermophoresis (MST) we found the ideal alternative and we were immediately convinced by the low sample consumption and immobilization-free setup.

Because of the scientific community being concerned about labeling Sirtuin enzymes or ligands, we further appreciated the truly label-free approach offered by the Monolith NT.LabelFree. We use this instrument mainly to characterize substrate and metabolite binding to the enzymes and to quantify the binding affinity of inhibitors and drug candidates. In addition, the Monolith NT.115 enables us to measure protein-protein interactions, which are difficult to assess with other methods because of the low protein amounts available.

Over the last years, we could gain a lot of essential information from our MST experiments enabling us to publish these comprehensive mechanistic insights together with high-resolution crystallographic data.

Finally, I would like to emphasize the customer-oriented attitude of this company. Their support team always has an open ear for our questions and offers help with challenging experiments. The company also appreciates our feedback on our experience with the technology and the instruments.

Prof. Dr. Clemens Steegborn, Head of the Biochemistry Department, University of Bayreuth, Germany