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A pyrene-linked protein cavity attracts two substrate molecules like the scent of a flower attracts butterflies. In their Communication (DOI: 10.1002/anie.201704524), A. Onoda, T. Hayashi, and co-workers demonstrate that a polycyclic pyrene moiety linked within the rigid protein scaffold of the ?-barrel of nitrobindin acts as a platform to provide an aromatic interaction with a substrate.
A unique ?-expanded reaction cavity tethering a polycyclic moiety which provides a platform for substrate binding was constructed within the robust ?-barrel structure of nitrobindin (NB). NB variants with cavities of different sizes and shapes are coupled with N-(1-pyrenyl)maleimide (Pyr) to prepare a series of NB-Pyr conjugates. The orientation of the pyrene moiety is fixed within the cavity by the coupling reaction.
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