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Microscale thermophoresis paves way for new drug-screening assay

copyright by NANOTEMPER

G-Protein Coupled Receptors are a very elegant and potentially revolutionary new way to screen for drugs binding to membrane receptors.

Microscale Thermophoresis (MST) is a powerful new technology, and easy to handle. It detects changes in the hydration shell of molecules and measures enzyme activities and bio-molecule interactions under close-tonative conditions: immobilization-free and in bio-liquids of choice.

Customer Requirements

Infrared-lasers are used to produce precise microscale temperature gradients within thin glass capillaries that are filled with a solution of choice (buffer or serum, cell lysate and other bioliquids). Molecules move along these temperature gradients.

Based on the proprietary technology “Microscale Thermophoresis (MST)”,  NanoTemper is developing affordable analytical instruments for the characterization of biomolecule interactions and for the study of biomolecule activity in vitro. The instruments are suited for basic research and pharmaceutical applications.

Receptor proteins located within the cell membrane serve to convey molecules or information into the interior. Because numerous drugs function by binding to such receptors, their interactions play important roles in the fight against various diseases. For example, the coupling can activate a signal chain which in the end specifically changes the metabolism of malignant cells.

Our solution

The technology uses a fluorescence microscope equipped with a dichroic mirror that couples a IR-Laser into the path of fluorescence light. The heating laser is focused with the same objective used for fluorescence detection. This enables a precise local heating (1-6 K) of the glass capillary and simultaneously to observe and measure local changes of fluorescence intensity due to the motion of labeled molecules in the glass capillaries.

Fluorescently labeled molecules or particles are initially distributed evenly and diffuse freely in solution. By switching on the IR-Laser, the molecules experience a thermophoretic force in the temperature gradient and typically move out of the heated spot. In the steady state, this molecule flow is counterbalanced by ordinary mass diffusion. After turning off the laser, the particles diffuse back towards a homogeneous distribution.

The following stages are recorded for each sample: fluorescence signal before turning the IR laser on, fast temperature-dependent changes in fluorescence intensity of the analyzed molecules, thermophoresis and back diffusion after switching the laser off.

Customer Statement

"The method is so sensitive that small, binding-induced changes in the conformation or shape of a GPCR can be detected using very small amounts of protein and test sample. By varying the amount of drug, the efficacy of the binding can be determined quantitatively.
The new approach has great potential to become a simple and rapid standard assay for pharmaceutical and basic research (NIM)."
Dr. Philipp Baaske, NanoTemper

 

"This project with NanoTemper and AMS Technologies is the kind of cooperation we are focussed on: Innovative applications with special needs and good growth potential. Partners in Fiberoptics means to help our customers to concentrate on their application and their business while joining with our expertise in opto-electronics. NanoTemper as a young, fast growing venture is early developing visions for future product generations and we are involved at an early design stage and even in the discussion of these visions."
Dr. Gerald Werner, Fibotec Fiberoptics GmbH, www.fibotec.com

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