Conformational photoswitching of a synthetic peptide foldamer bound within a phospholipid bilayer

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Science  29 Apr 2016:
Vol. 352, Issue 6285, pp. 575-580
DOI: 10.1126/science.aad8352

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Synthetic twists among lipids

Proteins embedded in cell membranes perform a wide variety of signaling and transport functions through conformational shifts. De Poli et al. examined how a much smaller, simpler construct might begin to achieve similar aims (see the Perspective by Thiele and Ulrich). Specifically, they designed an artificial peptide with a photosensitive group at one end and embedded it in a phospholipid bilayer akin to a membrane. Nuclear magnetic resonance spectroscopy revealed how light-induced isomerization influenced conformational dynamics at the other end. The results point the way toward development of small-molecule–based switches in membrane environments.

Science, this issue p. 575; see also p. 520


The dynamic properties of foldamers, synthetic molecules that mimic folded biomolecules, have mainly been explored in free solution. We report on the design, synthesis, and conformational behavior of photoresponsive foldamers bound in a phospholipid bilayer akin to a biological membrane phase. These molecules contain a chromophore, which can be switched between two configurations by different wavelengths of light, attached to a helical synthetic peptide that both promotes membrane insertion and communicates conformational change along its length. Light-induced structural changes in the chromophore are translated into global conformational changes, which are detected by monitoring the solid-state 19F nuclear magnetic resonance signals of a remote fluorine-containing residue located 1 to 2 nanometers away. The behavior of the foldamers in the membrane phase is similar to that of analogous compounds in organic solvents.

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