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. FIND THE PAPER HERE Instrument: Fluidity One Therapeutic area: Peptide-lipid interactions A full list of recent publications in which our technology has been applied can be accessed here.