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

Andrew J. Wilson, James R. Ault, Maria H. Filby, Hazel I. A. Phillips, Alison E. Ashcroft, Nicholas C. Fletcher

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)
199 Downloads (Pure)


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.
Original languageEnglish
Pages (from-to)2206-2212
Number of pages7
JournalOrganic and Biomolecular Chemistry
Issue number13
Early online date30 Jan 2013
Publication statusPublished - 2013

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Biochemistry


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