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Updated: May 14, 2026

The Synthesis, Characterization and Reactivity of a Series of Ruthenium N-triphosPh Complexes
Published on: April 10, 2015
Protein destabilisation by ruthenium(II) tris-bipyridine based protein-surface mimetics
Andrew J Wilson1, James R Ault, Maria H Filby
1School of Chemistry, University of Leeds, Woodhouse Lane, Leeds LS2 9JT, United Kingdom. A.J.Wilson@leeds.ac.uk
None:
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.
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