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Issue 13, 2013
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Protein destabilisation by ruthenium(II) tris-bipyridine based protein-surface mimetics

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Abstract

Highly functionalised ruthenium(II) tris-bipyridine receptor 1 which acts as a selective sensor for equine cytochrome c (cyt c) is shown to destabilise the native protein conformation by around 25 °C. Receptors 2 and 3 do not exert this effect confirming the behaviour is a specific effect of molecular recognition between 1 and cyt c, whilst the absence of a destabilising effect on 60% acetylated cyt c demonstrates the behaviour of 1 to be protein specific. Molecular recognition also modifies the conformational properties of the target protein at room temperature as evidenced by ion-mobility spectrometry (IMS) and accelerated trypsin proteolysis.

Graphical abstract: Protein destabilisation by ruthenium(ii) tris-bipyridine based protein-surface mimetics

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Publication details

The article was received on 01 Jul 2012, accepted on 29 Jan 2013 and first published on 30 Jan 2013


Article type: Paper
DOI: 10.1039/C3OB26251K
Citation: Org. Biomol. Chem., 2013,11, 2206-2212
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    Protein destabilisation by ruthenium(II) tris-bipyridine based protein-surface mimetics

    A. J. Wilson, J. R. Ault, M. H. Filby, H. I. A. Philips, A. E. Ashcroft and N. C. Fletcher, Org. Biomol. Chem., 2013, 11, 2206
    DOI: 10.1039/C3OB26251K

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