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Article

Characterization of DAG Binding to TRPC Channels by Target-Dependent cis–trans Isomerization of OptoDArG

1
Gottfried Schatz Research Center for Cell Signaling, Metabolism and Aging—Division of Biophysics, Medical University Graz, 8010 Graz, Austria
2
Max Planck Institute of Colloids and Interfaces, 14476 Potsdam, Germany
3
Institute for Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany
4
Institute of Pharmacology, Center for Physiology and Pharmacology, Medical University of Vienna, 1090 Vienna, Austria
*
Authors to whom correspondence should be addressed.
Academic Editor: Alessandro Alaimo
Biomolecules 2022, 12(6), 799; https://doi.org/10.3390/biom12060799
Received: 6 May 2022 / Revised: 3 June 2022 / Accepted: 5 June 2022 / Published: 7 June 2022
(This article belongs to the Special Issue Lipid-Gating and Lipid-Protein Interactions in Ion Channels)
Azobenzene-based photochromic lipids are valuable probes for the analysis of ion channel–lipid interactions. Rapid photoisomerization of these molecules enables the analysis of lipid gating kinetics and provides information on lipid sensing. Thermal relaxation of the metastable cis conformation to the trans conformation of azobenzene photolipids is rather slow in the dark and may be modified by ligand–protein interactions. Cis photolipid-induced changes in pure lipid membranes as visualized from the morphological response of giant unilamellar vesicles indicated that thermal cis–trans isomerization of both PhoDAG-1 and OptoDArG is essentially slow in the lipid bilayer environment. While the currents activated by cis PhoDAG remained stable upon termination of UV light exposure (dark, UV-OFF), cis OptoDArG-induced TRPC3/6/7 activity displayed a striking isoform-dependent exponential decay. The deactivation kinetics of cis OptoDArG-induced currents in the dark was sensitive to mutations in the L2 lipid coordination site of TRPC channels. We conclude that the binding of cis OptoDArG to TRPC channels promotes transition of cis OptoDArG to the trans conformation. This process is suggested to provide valuable information on DAG–ion channel interactions and may enable highly selective photopharmacological interventions. View Full-Text
Keywords: lipid photopharmacology; TRPC channels; diacylglycerols; photoisomerization lipid photopharmacology; TRPC channels; diacylglycerols; photoisomerization
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MDPI and ACS Style

Erkan-Candag, H.; Krivic, D.; Gsell, M.A.F.; Aleksanyan, M.; Stockner, T.; Dimova, R.; Tiapko, O.; Groschner, K. Characterization of DAG Binding to TRPC Channels by Target-Dependent cis–trans Isomerization of OptoDArG. Biomolecules 2022, 12, 799. https://doi.org/10.3390/biom12060799

AMA Style

Erkan-Candag H, Krivic D, Gsell MAF, Aleksanyan M, Stockner T, Dimova R, Tiapko O, Groschner K. Characterization of DAG Binding to TRPC Channels by Target-Dependent cis–trans Isomerization of OptoDArG. Biomolecules. 2022; 12(6):799. https://doi.org/10.3390/biom12060799

Chicago/Turabian Style

Erkan-Candag, Hazel, Denis Krivic, Mathias A. F. Gsell, Mina Aleksanyan, Thomas Stockner, Rumiana Dimova, Oleksandra Tiapko, and Klaus Groschner. 2022. "Characterization of DAG Binding to TRPC Channels by Target-Dependent cis–trans Isomerization of OptoDArG" Biomolecules 12, no. 6: 799. https://doi.org/10.3390/biom12060799

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