Photoswitching of model ion channels in lipid bilayers
| Autor: | Timur R. Galimzyanov, Christof Hannesschlaeger, Toma N. Glasnov, Sergey A. Akimov, Peter Pohl, Juergen Pfeffermann, Georg Pabst, Barbara Eicher, Danila Boytsov |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Radiation
Radiological and Ultrasound Technology Photoisomerization Light Chemistry Vesicle Bilayer Lipid Bilayers Biophysics Gramicidin Conductance Membrane Proteins Ion Channels Membrane protein Isomerism X-Ray Diffraction Scattering Small Angle Radiology Nuclear Medicine and imaging Mechanosensitive channels Lipid bilayer Ion channel |
| Zdroj: | Journal of photochemistry and photobiology. B, Biology. 224 |
| ISSN: | 1873-2682 |
| Popis: | Membrane proteins can be regulated by alterations in material properties intrinsic to the hosting lipid bilayer. Here, we investigated whether the reversible photoisomerization of bilayer-embedded diacylglycerols (OptoDArG) with two azobenzene-containing acyl chains may trigger such regulatory events. We observed an augmented open probability of the mechanosensitive model channel gramicidin A (gA) upon photoisomerizing OptoDArG's acyl chains from trans to cis: integral planar bilayer conductance brought forth by hundreds of simultaneously conducting gA dimers increased by typically >50% - in good agreement with the observed increase in single-channel lifetime. Further, (i) increments in the electrical capacitance of planar lipid bilayers and protrusion length of aspirated giant unilamellar vesicles into suction pipettes, as well as (ii) changes of small-angle X-ray scattering of multilamellar vesicles indicated that spontaneous curvature, hydrophobic thickness, and bending elasticity decreased upon switching from trans- to cis-OptoDArG. Our bilayer elasticity model for gA supports the causal relationship between changes in gA activity and bilayer material properties upon photoisomerization. Thus, we conclude that photolipids are deployable for converting bilayers of potentially diverse origins into light-gated actuators for mechanosensitive proteins. |
| Databáze: | OpenAIRE |
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