Know more

Our use of cookies

Cookies are a set of data stored on a user’s device when the user browses a web site. The data is in a file containing an ID number, the name of the server which deposited it and, in some cases, an expiry date. We use cookies to record information about your visit, language of preference, and other parameters on the site in order to optimise your next visit and make the site even more useful to you.

To improve your experience, we use cookies to store certain browsing information and provide secure navigation, and to collect statistics with a view to improve the site’s features. For a complete list of the cookies we use, download “Ghostery”, a free plug-in for browsers which can detect, and, in some cases, block cookies.

Ghostery is available here for free:

You can also visit the CNIL web site for instructions on how to configure your browser to manage cookie storage on your device.

In the case of third-party advertising cookies, you can also visit the following site:, offered by digital advertising professionals within the European Digital Advertising Alliance (EDAA). From the site, you can deny or accept the cookies used by advertising professionals who are members.

It is also possible to block certain third-party cookies directly via publishers:

Cookie type

Means of blocking

Analytical and performance cookies

Google Analytics

Targeted advertising cookies


The following types of cookies may be used on our websites:

Mandatory cookies

Functional cookies

Social media and advertising cookies

These cookies are needed to ensure the proper functioning of the site and cannot be disabled. They help ensure a secure connection and the basic availability of our website.

These cookies allow us to analyse site use in order to measure and optimise performance. They allow us to store your sign-in information and display the different components of our website in a more coherent way.

These cookies are used by advertising agencies such as Google and by social media sites such as LinkedIn and Facebook. Among other things, they allow pages to be shared on social media, the posting of comments, and the publication (on our site or elsewhere) of ads that reflect your centres of interest.

Our EZPublish content management system (CMS) uses CAS and PHP session cookies and the New Relic cookie for monitoring purposes (IP, response times).

These cookies are deleted at the end of the browsing session (when you log off or close your browser window)

Our EZPublish content management system (CMS) uses the XiTi cookie to measure traffic. Our service provider is AT Internet. This company stores data (IPs, date and time of access, length of the visit and pages viewed) for six months.

Our EZPublish content management system (CMS) does not use this type of cookie.

For more information about the cookies we use, contact INRA’s Data Protection Officer by email at or by post at:

24, chemin de Borde Rouge –Auzeville – CS52627
31326 Castanet Tolosan CEDEX - France

Dernière mise à jour : Mai 2018

Menu Institutions

SPS - Saclay Plant Sciences

Thermophoresis: an innovative method for biomolecular interaction analysis

A MicroScaleThermophoresis (MST) device, co-funded by the SPS LabEx, AgroParisTech, the “Ile de France” region and the Jean-Pierre Bourgin Institute (IJPB), has been acquired in 2015, to equip the Plant Observatory Biochemistry platform of the IJPB at the INRA site of Versailles. Through the Plant Observatory, the MST technique is available to all the scientists of the SPS LabEx, the research/teaching community of the Université Paris-Saclay and all our academic partners.

Thermophoresis, or Soret effect, measures the directed motion of molecules in a temperature gradient. The movement of a compound in solution depends on various molecular properties such as size, charge, and hydration shell according to the Soret law. When two molecules interact, at least one of these parameters is modified, resulting in a modification of the thermophoresis curve.

Based on the thermophoresis principle, MST is a cutting-edge and easy to handle technology developed to study and quantify the interactions between diverse biomolecules, purified or not.

The equipment we acquired makes it possible to detect variations in the thermophoretic mobility of a fluorescent molecule (naturally or by fluorescent labeling) subjected to a micro gradient of temperature established in a capillary, in the presence of increasing concentrations of a specific interacting agent. Exploiting the thermophoretic properties of a compound for molecular interaction studies is an innovative approach.


(A) MST equipment (Monolith NT.115 from NanoTemper Technologies GmbH). (B) Schematic representation of MST optics. The fluorescence within the capillaries (16 capillaries of ∼4 μL) is excited and measured through the same optical device. A focused IR-Laser heats locally and the thermophoresis of fluorescent molecules through the temperature gradient is detected (C) Initially, the molecules are homogeneously distributed and a constant “initial fluorescence” is recorded. After activation of the IR laser, the thermophoretic movement of the fluorescencently labeled molecules out of the heated sample volume can be measured. After deactivation of the IR-Laser, a “backdiffusion” of molecules occurs, solely driven by mass diffusion. (D) Typical binding experiment. The thermophoretic movement of a fluorescent molecule (black trace; “unbound”) changes upon binding to a non-fluorescent ligand (red trace; “bound”), resulting in different traces. Titration of the non-fluorescent ligand results in a gradual change in thermophoresis, which is plotted as ΔFnorm to generate a binding curve, which can be fitted to derive binding constants.

Beyond its simplicity of implementation, the MST technique has many advantages, including:

  • Sensitivity: the method is based on the recording of minimal variations in mass, charge or solvation. It allows the measurement of interactions with essentially no limitation on molecule size.
  • Measurements in solution: contrary to other techniques of interaction studies, no immobilization is required and therefore no conformational disturbance is to be feared.
  • Very wide application ranges: protein / protein, protein / ligand, protein / sugar, protein / DNA, ligand / viral particle, bacteria, cell, etc.
  • Fluorescent labeling of a purified protein: the labeling, either on lysines or on cysteines contained in the protein, can be achieved in less than one hour.
  • Purification of the molecules not always required: for example, GFP-fusion proteins can be analyzed directly in cell extracts without purification, which is interesting if cellular partners are needed for the interaction  (partner protein, cofactor, etc.)
  • Possibility to use the fluorescence of different molecules, labeled nucleic acids or oligosaccharides, for example.
  • Use of low amount of the labeled species: 10 μl of a pM to nM solution, with a large dynamic range of dissociation constants (KD 10-11 to 10-2 M).
  • Rapidity: different experimental conditions can be tested quickly, such as pH, in the presence of salts, detergents etc., or the type of capillary (standard or substituted). Once the experimental conditions are established, the dissociation constants can be obtained in 10 min.
  • Relatively low cost consumables: about 300 € for 1000 standard capillaries.
  • Intuitive data acquisition and processing software.

MST requires rigor and precision, particularly with regard to the distribution of the fluorescent partner, but its simplicity of use nevertheless makes it possible to propose this method of interaction study on a technical platform after a short training. MST can also allow students to understand the notion of specific interaction and to experimentally measure dissociation constants.

Since the acquisition of the MST equipment, IJPB scientists have obtained encouraging results in various research programs and others are being published. Interactions between receptors and peptide ligands, or receptor and hormone, or between a transcription factor and its DNA target have been highlighted.

The Plant Observatory welcomes SPS LabEx scientists in order to help them become familiar with this technique, to initiate preliminary assays together and to study if MST is a relevant technique for the potential molecular interactions studied.



Reference article :

Wienken CJ, Baaske P, Rothbauer U, Braun D, Duhr S. Protein-binding assays in biological liquids using microscale thermophoresis. Nat Commun. 2010 Oct 19;1:100. doi: 10.1038/ncomms1093. PMID: 20981028

Protein/protein interaction:

Chen ST, He NY, Chen JH, Guo FQ. Identification of core subunits of photosystem II as action sites of HSP21, which is activated by the GUN5-mediated retrograde pathway in Arabidopsis. Plant J. 2017 89(6):1106-1118. doi:10.1111/tpj.13447. Epub 2017 Feb 27. PubMed PMID: 27943531.

Sénéchal F, L'Enfant M, Domon JM, Rosiau E, Crépeau MJ, Surcouf O, Esquivel-Rodriguez J, Marcelo P, Mareck A, Guérineau F, Kim HR, Mravec J, Bonnin E, Jamet E, Kihara D, Lerouge P, Ralet MC, Pelloux J, Rayon C. Tuning of Pectin Methylesterification: Pectin methylesterase inhibitor 7 modulates the processive activity of co-expressed pectin methylesterase 3 in a PH-dependent manner. J Biol Chem. 2015 290(38):23320-35. doi: 10.1074/jbc.M115.639534. Epub 2015 Jul16. PubMed PMID: 26183897; PubMed Central PMCID: PMC4645611.

Protein / small organic compound interaction:

Zhang W, Li X, Zhang G, Ding Y, Ran L, Luo L, Wu J, Hu D, Song B. Binding interactions between enantiomeric α-aminophosphonate derivatives and tobacco mosaic virus coat protein. Int J Biol Macromol. 2017 Jan;94(Pt A):603-610. doi: 10.1016/j.ijbiomac.2016.10.027. Epub 2016 Oct 13. PubMed PMID: 27746356.

Protein / nucleic acid interaction:

Girke C, Arutyunova E, Syed M, Traub M, Möhlmann T, Lemieux MJ. High yield expression and purification of equilibrative nucleoside transporter 7 (ENT7) from Arabidopsis thaliana. Biochim Biophys Acta. 2015 1850(9):1921-9. doi: 10.1016/j.bbagen.2015.06.003. Epub 2015 Jun 12. PubMed PMID: 26080001.

Protein / ion interaction:

Parker JL, Newstead S. Molecular basis of nitrate uptake by the plant nitrate transporter NRT1.1. Nature. 2014 507(7490):68-72. doi: 10.1038/nature13116. Epub 2014 Feb 26. PMID: 24572366