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  Characterization of DAG binding to TRPC channels by target-dependent cis–trans isomerization of OptoDArG

Erkan-Candag, H., Krivic, D., Gsell, M. A. F., Aleksanyan, M., Stockner, T., Dimova, R., et al. (2022). Characterization of DAG binding to TRPC channels by target-dependent cis–trans isomerization of OptoDArG. Biomolecules, 12(6): 799. doi:doi:10.3390/biom12060799.

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 Creators:
Erkan-Candag, Hazel, Author
Krivic, Denis1, Author              
Gsell, Mathias A. F., Author
Aleksanyan, Mina1, Author              
Stockner, Thomas, Author
Dimova, Rumiana1, Author              
Tiapko, Oleksandra, Author
Groschner, Klaus, Author
Affiliations:
1Rumiana Dimova, Kolloidchemie, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_3360040              

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Free keywords: lipid photopharmacology; TRPC channels; diacylglycerols; photoisomerization
 Abstract: 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.

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Language(s): eng - English
 Dates: 2022-06-072022
 Publication Status: Published in print
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 Identifiers: DOI: doi:10.3390/biom12060799
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Title: Biomolecules
Source Genre: Journal
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Publ. Info: Basel, Switzerland : MDPI
Pages: - Volume / Issue: 12 (6) Sequence Number: 799 Start / End Page: - Identifier: ISSN: 2218-273X