Remote-control of the enantiomeric supramolecular recognition mediated by chiral azobenzenes bound to human serum albumin.

Three novel tyrosine-conjugated azobenzene molecules were designed and their ability to target a natural chiral host matrix (human serum albumin, HSA) was investigated. We found that the interplay between the spatial configuration of the chiral substituents and the change in local symmetry resulting from the photoisomerization process strongly affects the optical activity of the bound photochromes. In particular, the different signal amplification obtained upon binding of the photoswitches to the biopolymer enables obtaining a chirooptical system tunable over a wide range of wavelengths.