4.8 Article

How Photoswitchable Lipids Affect the Order and Dynamics of Lipid Bilayers and Embedded Proteins

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JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 143, 期 25, 页码 9515-9528

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AMER CHEMICAL SOC
DOI: 10.1021/jacs.1c03524

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  1. Deutsche Forschungsgemeinschaft Graduate School CLiC (Complex Light Control) [GRK 1986]

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Altering the properties of phospholipid membranes by light is an attractive option for noninvasive manipulation of membrane proteins and cellular functions, with the study finding efficient trans-to-cis conversion in liposomes containing AzoPC under UV-light illumination, resulting in a localized reduction of the CH order parameter within the bulk lipid acyl chains. This study demonstrates the concept of using photoswitchable lipids to modulate membrane properties by light for inducing dynamic changes within an embedded membrane protein.
Altering the properties of phospholipid membranes by light is an attractive option for the noninvasive manipulation of membrane proteins and cellular functions. Lipids with an azobenzene group within their acyl chains such as AzoPC are suitable tools for manipulating lipid order and dynamics through a light-induced trans-to-cis isomerization. However, the action of these photoswitchable lipids at the atomic level is still poorly understood. Here, liposomes containing AzoPC, POPE, and POPG have been characterized by solid-state NMR through chemical shift and dipolar CH order parameter measurements. Upon UV-light illumination, an efficient trans-to-cis conversion can be achieved resulting in a localized reduction of the CH order parameter within the bulk lipid acyl chains. This effect is even more pronounced in liposomes containing the integral membrane protein E. coli diacylglycerol kinase. The protein responds to the light-induced trans-to-cis isomerization by a site-specific increase in the molecular dynamics as observed by altered cross peak intensities in NCA spectra. This study represents a proof-of-concept demonstration for the use of photoswitchable lipids to modulate membrane properties by light for inducing dynamic changes within an embedded membrane protein.

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