Publication

Putative interaction site for membrane phospholipids controls activation of TRPA1 channel at physiological membrane potentials.

Lucie Macikova, Viktor Sinica, Anna Kadkova, Sandrine Villette, Alexandre Ciaccafava, Jonathan Faherty, Sophie Lecomte, Isabel D. Alves, Viktorie Vlachova.

The FEBS Journal 14931, 2019 May 20

Macikova et al use Microfluidic Diffusional Sizing (MDS) along with other techniques to understand the role phosphatidylinositol-4,5-bisphosphate (PIP2) has in the regulation of transient receptor potential ankyrin 1 (TRPA1) channel. The Fluidity One was used to create binding curves of the interactions between two specific peptides (L992-N1008 and T1003-P1034) and model lipid membranes in the presence of PIP2.

The paper demonstrates that the two peptides (L992-N1008 and T1003-P1034) interact with lipid membranes only if PIP2 is present and their affinities depend on the presence of calcium. The paper also shows tht the putative phosphoinositide-interacting domain contributes to the stabilization of the TRPA1 channel gate.

binding curves from macikova et al 2019

Fig 1. shows the binding curves obtained using the Fluidity One for each of the two peptides binding to the lipid membrane in the presence of PIP2.

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