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Friday, 22 October, 2010

Monitoring asymmetric molecular encounters

New method can detect binding interactions in blood samples

 

© Nature Communications 1, 2010

Chemical compounds with low molecular weights (“small molecules”) are ideal starting points for the development of novel pharmacological agents. Their small size facilitates entry into cells, where they must act, usually by binding to proteins that are much larger than they are. A research team consisting of LMU biophysicist Professor Dieter Braun and scientists at NanoTemper Technologies GmbH, an LMU spin-off, have developed a new method that can detect and quantify interactions between molecules of widely different sizes. The technique makes use of “Microscale Thermophoresis” (MST), which is sensitive to the electrical charge of molecule changes of the hydration spheres (bound layers of water) associated with them. “We can now analyze binding interactions between molecules, essentially irrespective of the size differences between the partners involved”, says Braun. “This allows us to monitor the binding of ions or small-molecule interactors to proteins, and by using fluorescent dyes as markers, we can study binding in blood and other complex biological fluids.” The new method was developed in cooperation with NanoTemper Technologies, and the study was supported by the Cluster of Excellence “Nanosystems Initiative Munich” (NIM).

 

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Publication "Protein-binding assays in biological liquids using microscale thermophoresis"