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Updated: Feb 22, 2026
Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions
Published on: February 10, 2022
Caracterización de las interacciones lípidicas de Akt1 humana mediante fluorimetría de barrido diferencial sin
Obada Bahra1, Michal Grzybek2, Ünal Coskun3
1Center of Membrane Biochemistry and Lipid Research, University Hospital and Faculty of Medicine Carl Gustav Carus; TU Dresden, Dresden, Germany; Paul Langerhans Institute Dresden (PLID) of the Helmholtz Center Munich at the University Hospital Carl Gustav Carus and Faculty of Medicine of the TU Dresden, Dresden, Germany; German Center for Diabetes Research (DZD), Neuherberg, Germany.
Abstract:
Understanding the role of lipids in protein function is key to obtaining details about cellular signaling pathways. Among the various methods available, label-free differential scanning fluorimetry has several advantages. This technique uses the intrinsic fluorescence of tryptophan and tyrosine residues, requires minute sample amounts, enables rapid, high-throughput analysis, and allows direct comparison of protein-lipid interactions in lipid bilayers and with water-soluble lipid analogues. Here, we present a detailed protocol for monitoring the interaction between human full-length Akt1 and phosphatidylinositol-3,4,5-trisphosphate (PIP3), either in solution with short-chain PIP3 (4:0/4:0) or within membranes containing PIP3 (16:0/16:0). This versatile protocol can easily be adapted to study other protein-ligand interactions.
