β-Cyclodextrin as a mimetic of the natural GFP-chromophore environment

The green fluorescent protein (GFP) chromophore has been anchored to β-cyclodextrin (βCD) via a copper(I)-catalyzed azide-alkyne cycloaddition. The photophysical properties of this new GFP-CD derivative have been evaluated, showing the formation of a self-inclusion complex and enhancement of fluorescence of the GFP-chromophore covalently bound to the βCD. This enhancement of fluorescence by encapsulation and hence fixation of the chromophore in a binding pocket mimics the effect exerted by the natural protein environment.