RESUMO
The metal hydration state within a designed coiled coil can be progressively tuned across the full integer range (3 â 0 aqua ligands), by careful choice of a second sphere terminal residue, including the lesser used Trp. Potential implications include a four-fold change in MRI relaxivity when applied to lanthanide coiled coils.
Assuntos
Complexos de Coordenação/química , Gadolínio/química , Peptídeos/química , Sequência de Aminoácidos , Sítios de Ligação , Ligação ProteicaRESUMO
Herein the first example of a bimetallic coiled coil featuring a lanthanide binding site is reported, opening opportunities to exploit the attractive NMR and photophysical properties of the lanthanides in multi metallo protein design. In our efforts to fully characterise the system we identified for the first time that lanthanide binding to such sites is pH dependent, with optimal binding at neutral pH, and that the double AsnAsp site is more versatile in this regard than the single Asp site. Our second site featured the structural HgCys3 site, the chemistry of which was essentially unaltered by the presence of the lanthanide site. In fact, both metal binding sites within the hetero bimetallic coiled coil displayed the same properties as their mononuclear single binding site controls, and operated independently of each other. Finally, pH can be used as an external trigger to control the binding of Hg(ii) and Tb(iii) to the two distinct sites within this coiled coil, and offers the opportunity to "activate" metal binding sites within complex multi metallo and multi-functional designs.