The use of light-responsive proteins to control both living or synthetic cells, is at the core of the expanding fields of optogenetics and synthetic biology. It is thus apparent that a richer reaction toolbox for the preparation of such systems is of fundamental importance. Here, we provide a proof-of-principle demonstration that Morita-Baylis-Hillman adducts can be employed to perform a facile site-specific, irreversible and diastereoselective click-functionalization of a lysine residue buried into a lipophilic binding pocket and yielding an unnatural chromophore with an extended π-system. In doing so we effectively open the path to the in vitro preparation of a library of synthetic proteins structurally reminiscent of xanthopsin eubacterial photoreceptors. We argue that such a library, made of variable unnatural chromophores inserted in an easy-to-mutate and crystallize retinoic acid transporter, significantly expand the scope of the recently introduced rhodopsin mimics as both optogenetic and “lab-on-a-molecule” tools.

Tassone, G., Paolino, M., Pozzi, C., Reale, A., Salvini, L., Giorgi, G., et al. (2022). Xanthopsin-like systems via site-specific click-functionalization of a retinoic acid binding protein. CHEMBIOCHEM, 23(1) [10.1002/cbic.202100449].

Xanthopsin-like systems via site-specific click-functionalization of a retinoic acid binding protein

Tassone G.;Paolino M.
;
Pozzi C.;Reale A.;Giorgi G.;Orlandini M.;Galvagni F.;Mangani S.;Olivucci M.
;
Cappelli A.
2022-01-01

Abstract

The use of light-responsive proteins to control both living or synthetic cells, is at the core of the expanding fields of optogenetics and synthetic biology. It is thus apparent that a richer reaction toolbox for the preparation of such systems is of fundamental importance. Here, we provide a proof-of-principle demonstration that Morita-Baylis-Hillman adducts can be employed to perform a facile site-specific, irreversible and diastereoselective click-functionalization of a lysine residue buried into a lipophilic binding pocket and yielding an unnatural chromophore with an extended π-system. In doing so we effectively open the path to the in vitro preparation of a library of synthetic proteins structurally reminiscent of xanthopsin eubacterial photoreceptors. We argue that such a library, made of variable unnatural chromophores inserted in an easy-to-mutate and crystallize retinoic acid transporter, significantly expand the scope of the recently introduced rhodopsin mimics as both optogenetic and “lab-on-a-molecule” tools.
2022
Tassone, G., Paolino, M., Pozzi, C., Reale, A., Salvini, L., Giorgi, G., et al. (2022). Xanthopsin-like systems via site-specific click-functionalization of a retinoic acid binding protein. CHEMBIOCHEM, 23(1) [10.1002/cbic.202100449].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/1186435