Measure and compare biomolecular interactions within simple glass capillaries.
Investigate the binding affinities of a broad range of biomolecules
We offer a robust and easy to handle system based on microscale thermophoresis, which allows measurements without extensive preparations and setup procedures. Ideally you can get basic results within a few hours. The machine is easy to handle, robust and the experimental method straightforward. The system is suitable for assisted access.
Microscale Thermophoresis MST
Microscale Thermophoresis is a new powerful technology which can be used to measure biomolecular interactions. The basic underlying principle Thermophoresis is the movement of biomolecules along a temporarily induced tiny temperature gradient. Binding events affect the thermophoretic movement of the involved molecules. The molecular movement can be monitored in simple glass capillaries with optical methods. The powerful technology has been developed by the Munich based company Nano Temper. An infrared-laser is used to induce a precise microscopic temperature gradient (2-5 K) within the glass capillary. At the Nano Temper website you can find a short introduction into Microscale Thermophoresis and numerous application examples.
The advantages of the method are:
Immobilization-free in buffer of choice
Fast measurement of dissociation constants
Low sample consumption
Inexpensive and easy to handle
Robust technology which allows assisted access
Low running costs
In our facility we have a Nano Temper Monolith NT 115 machine which is suitable for assisted access for internal users (please use the contact form right hand for request) .
The NT115 has a fluorescence detection system with the option to switch between two filter settings (red/blue).
Available filter settings and examples of appropriate fluorescence dyes
The fluorescent component is measured against a dilution series of the binding partner (titrant).
Nano Temper offers also a label free instrument, which relies on tryptophane fluorescence and requires significant differences in tryptophane content within the analytes.
We decided in favor of the fluorescence labeling based technology, because it can be applied to a broad range of biomolecules such as:
Protein - Protein
Protein - Peptide
Protein - DNA/RNA
Protein - Oligosaccharides
Protein - Liposomes
Protein - Ribosome
Protein - small molecules
Protein - Organelles
Protein - Virus particles
At the following page you can find a short description of the practical aspects and the workflow.