Microscale thermophoresis in the investigation of biomolecular interactions

doi:10.5246/jcps.2020.09.061

Abstract

Abstract:

Accurate characterization of the interactions between biomolecules not only provides fundamental insights into cellular processes but also paves the way for drug discovery and development. With recent increases in throughput and sensitivity, biophysical technologies have become prominent tools for studying biomolecular interactions. Biophysical techniques that can reduce costs, shorten detection time, simplify the complexity of the system under analysis, and simultaneously provide high-quality data content are particularly favored. Here, we summarize the qualitative and quantitative analysis of biomolecular interactions using MicroScale Thermophoresis (MST), as well as extend the application of MST functions to explore thermodynamics, enzyme kinetics and protein folding-unfolding processes. MST has emerged as a simple and powerful biophysical approach for identifying and quantifying binding events based on the movement of molecules along microscopic temperature gradients. The advantages of MST over other competitive biophysical techniques include freedom from immobilization, rapid analysis times, lower sample consumption, and the ability to analyze binding affinities in cell lysates. This article discusses the instrumental setups, principles, experimental workflows, and examples of MST application in practice.

Key words: Biomolecular interactions, Biophysical technologies, MicroScale Thermophoresis

CLC Number:

R917

Supporting:

Qian Wang, Jing Wang, Shuxiang Song, Guiwang Zhu, Ze Cao, Zhenming Liu. Microscale thermophoresis in the investigation of biomolecular interactions[J]. Journal of Chinese Pharmaceutical Sciences, 2020, 29(9): 656-665.

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