Jump to main content
Jump to site search
PLANNED MAINTENANCE Close the message box

Scheduled maintenance work on Wednesday 27th March 2019 from 11:00 AM to 1:00 PM (GMT).

During this time our website performance may be temporarily affected. We apologise for any inconvenience this might cause and thank you for your patience.

Issue 13, 2013
Previous Article Next Article

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

Author affiliations


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

Back to tab navigation

Supplementary files

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
  • Open access:
  •   Request permissions

    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

Search articles by author