Publications

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

Published on July 24th, 2019

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

The FEBS Journal, 2019, 14931. DOI: 10.1111/febs.14931

Abstract

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 that the putative phosphoinositide-interacting domain contributes to the stabilization of the TRPA1 channel gate.

Figure 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.


Instrument: Fluidity One
Therapeutic area: Peptide-lipid interactions

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