Noncovalent interactions with proteins modify the physicochemical properties of a molecular switch

It is reported that spiropyran - a widely investigated molecular photoswitch - can 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. Turn me on: A photoswitchable spiropyran was stabilized in aqueous environments in the presence of a variety of proteins, including human serum albumin, insulin fibrils, lysozyme, and glucose oxidase. Depending on the protein, the spiropyran exhibited different physicochemical properties (see figure).