Microscale thermophoresis (MST) as a tool for measuring dynamin superfamily protein (DSP)–lipid interactions

Abstract

Microscale thermophoresis (MST) is a robust new fluorescence-based technology that enables measurement of biomolecular interactions and binding affinities (KD). MST is an immobilization-free alternative to surface plasmon resonance (SPR) and is cost-effective relative to isothermal titration calorimetry (ITC). In this chapter, using Drp1 as an example, we demonstrate for the first time, the application of MST to the determination of DSP–lipid interactions and the accurate measurement of KD under physiologically relevant solution conditions.