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. 2011 Jan 7;47(1):559-61.
doi: 10.1039/c0cc04754f. Epub 2010 Nov 23.

Protein surface recognition using geometrically pure Ru(II) tris(bipyridine) derivatives

Maria H Filby  1 , James Muldoon, Serin Dabb, Nicholas C Fletcher, Alison E Ashcroft, Andrew J Wilson
Affiliations

Protein surface recognition using geometrically pure Ru(II) tris(bipyridine) derivatives

Maria H Filby et al. Chem Commun (Camb). .

Abstract

This manuscript illustrates that the geometric arrangement of protein-binding groups around a ruthenium(II) core leads to dramatic differences in cytochrome c (cyt c) binding highlighting that it is possible to define synthetic receptors with shape complementarity to protein surfaces.

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Figures

Fig. 1
Fig. 1. Structures and proteins used in this study (a) cyt c (b) acetylated cyt c (c) α-chymoytrypsin (d) compounds 1 and 2.
Fig. 2
Fig. 2. (a) 1H NMR Spectra (500 MHz, d6-acetone) of tbutyl protected fac/mer Λ/Δ 1 and (b) circular dichroism spectra (CD) of fac/mer Λ/Δ 1 (H2O, pH 7.0, 100 μM).
Fig. 3
Fig. 3. Raw fluorescence data and titration curve for binding of Δ-mer 1 to cyt c.
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