Journal
CHEMPLUSCHEM
Volume 81, Issue 1, Pages 44-48Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cplu.201500417
Keywords
molecular switches; photochromism; photoisomerization; solvatochromism; spiropyrans
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Funding
- European Research Council [336080]
- Minerva Foundation
- G. M. J. Schmidt-Minerva Center for Supramolecular Architectures
- European Research Council (ERC) [336080] Funding Source: European Research Council (ERC)
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It is reported that spiropyrana widely investigated molecular photoswitchcan be stabilized in aqueous environments in the presence of a variety of proteins, including human serum albumin, insulin fibrils, lysozyme, and glucose oxidase. The optical properties of the complexed photoswitch are protein dependent, with human serum albumin providing the spiropyran with emission features previously observed for a photoswitch confined in media of high viscosity. Despite being bound to the protein molecules, spiropyran can undergo a ring-opening reaction upon exposure to UV light. This photoisomerization process can affect the properties of the proteins: here, it is shown that the electrical conduction through human serum albumin to which the spiropyran is bound increases following the ring-opening reaction.
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