Issue 13, 2013

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

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

Supplementary files

Article information

Article type
Paper
Submitted
11 شعبان 1433
Accepted
17 ربيع الأول 1434
First published
18 ربيع الأول 1434
This article is Open Access

Org. Biomol. Chem., 2013,11, 2206-2212

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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