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

Research output: Contribution to Journal/MagazineJournal articlepeer-review

  • Andrew J. Wilson
  • James R. Ault
  • Maria H. Filby
  • Hazel I. A. Philips
  • Alison E. Ashcroft
  • Nicholas C. Fletcher
<mark>Journal publication date</mark>7/04/2013
<mark>Journal</mark>Organic and Biomolecular Chemistry
Issue number13
Number of pages7
Pages (from-to)2206-2212
Publication StatusPublished
<mark>Original language</mark>English


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 degrees 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.