De novo designed ruthenium coiled coil metallopeptides Joseph Phillips, Anna Peacock University of Birmingham, UK
A new His-containing peptide sequence (H-pep) has been designed to bind to a widely studied Ru-catalyst precursor ([Ru(pcym)Cl2]2) by formation of a three-His binding site buried within a three-stranded coiled coil (CC)1-3. The designed CC binds two Ru-units and is the first de novo peptide to bind Ru to a preprogramed internal hydrophobic site. Fluorimetry and CD spectroscopy of H-pep and alanine control sequence (A-pep) mixtures support formation of heterotrimeric H-pep2:A-pep which has the same binding ratio to Ru as H-pep3, but with 1 less His-residue in the binding site. Mutation of the ‘spare’ position could tune substrate/solvent access to the Ru and, with the Ru-arene shown to be intact, there are opportunities for ligand modification/substitution prior to CC incorporation to further customise potential catalytic activity. References 1. Tegoni, F. Yu, M. Bersellini, J. E. Penner-Hahn and V. L. Pecoraro, Proc. Natl. Acad. Sci. U.S.A., 2012, 109, 21234–21239.
2. F. Yu, J. E. Penner-Hahn and V. L. Pecoraro, J.Am.Chem.Soc., 2013, 135, 18096–18107. 3. K. Suzuki, H. Hiroaki, D. Kohda, H. Nakamura and T. Tanaka, J.Am.Chem.Soc., 1998, 120,
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