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Reproducibility and accuracy of microscale thermophoresis in the NanoTemper Monolith: a multi laboratory benchmark study
B. López-Méndez, B. Baron, CA. Brautigam, TA. Jowitt, SH. Knauer, S. Uebel, MA. Williams, A. Sedivy, O. Abian, C. Abreu, M. Adamczyk, W. Bal, S. Berger, AK. Buell, C. Carolis, T. Daviter, A. Fish, M. Garcia-Alai, C. Guenther, J. Hamacek, J....
Language English Country Germany
Document type Journal Article
- MeSH
- Benchmarking * MeSH
- Calorimetry MeSH
- Laboratories * MeSH
- Reproducibility of Results MeSH
- Temperature MeSH
- Publication type
- Journal Article MeSH
Microscale thermophoresis (MST), and the closely related Temperature Related Intensity Change (TRIC), are synonyms for a recently developed measurement technique in the field of biophysics to quantify biomolecular interactions, using the (capillary-based) NanoTemper Monolith and (multiwell plate-based) Dianthus instruments. Although this technique has been extensively used within the scientific community due to its low sample consumption, ease of use, and ubiquitous applicability, MST/TRIC has not enjoyed the unambiguous acceptance from biophysicists afforded to other biophysical techniques like isothermal titration calorimetry (ITC) or surface plasmon resonance (SPR). This might be attributed to several facts, e.g., that various (not fully understood) effects are contributing to the signal, that the technique is licensed to only a single instrument developer, NanoTemper Technology, and that its reliability and reproducibility have never been tested independently and systematically. Thus, a working group of ARBRE-MOBIEU has set up a benchmark study on MST/TRIC to assess this technique as a method to characterize biomolecular interactions. Here we present the results of this study involving 32 scientific groups within Europe and two groups from the US, carrying out experiments on 40 Monolith instruments, employing a standard operation procedure and centrally prepared samples. A protein-small molecule interaction, a newly developed protein-protein interaction system and a pure dye were used as test systems. We characterized the instrument properties and evaluated instrument performance, reproducibility, the effect of different analysis tools, the influence of the experimenter during data analysis, and thus the overall reliability of this method.
Biochemistry 4 Biopolymers University of Bayreuth Universitaetsstr 30 95447 Bayreuth Germany
Biomolecular Analysis Core Facility University of Manchester Oxford Rd Manchester M13 9PL UK
Biozentrum University of Basel Klingelbergstrasse 50 70 4056 Basel Switzerland
Center for Molecular Biophysics UPR 4301 CNRS Orléans Rue Charles Sadron 45071 Orléans France
Department of Biochemistry Netherlands Cancer Institute Plesmanlaan 121 1066CX Amsterdam Netherlands
Department of Biochemistry University of Bayreuth Universitätsstr 30 95447 Bayreuth Germany
Department of Biochemistry University of Oxford South Parks Rd Oxford OX13 5LA UK
Departments of Biophysics and Microbiology UT Southwestern Medical Center Dallas TX 75390 USA
EMBL Hamburg Notkestrasse 85 22607 Hamburg Germany
Institut de Chimie Organique et Analytique CNRS FR 2708 UMR 7311 Université d'Orléans Orléans France
Institut de Recherches Servier 125 Chemin de Ronde 78290 Croissy sur Seine France
Institute of Biochemistry and Biophysics PAS Pawinskiego 5a 02 106 Warsaw Poland
Integrated Structural Biology Grenoble 71 avenue des Martyrs 38042 Grenoble Cedex 9 France
Max Planck Institute of Biochemistry Am Klopferspitz 18 Martinsried 82152 Planegg Germany
Molecular Biophysics Institut Pasteur 25 28 Rue du Dr Roux 75015 Paris France
NHLBI Biophysics Core Facility NHLBI NIH 50 South Dr Bethesda MD 20892 USA
ProteinTechnology Vienna Biocenter Core Facilities GmbH Dr Bohr Gasse 3 1030 Vienna Austria
Shared Research Facilities The Institute of Cancer Research London SW7 3RP UK
References provided by Crossref.org
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