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

Wilson, Andrew J. and Ault, James R. and Filby, Maria H. and Philips, Hazel I. A. and Ashcroft, Alison E. and Fletcher, Nicholas C. (2013) Protein destabilisation by ruthenium(II) tris-bipyridine based protein-surface mimetics. Organic and Biomolecular Chemistry, 11 (13). pp. 2206-2212. ISSN 1477-0520

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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.

Item Type:
Journal Article
Journal or Publication Title:
Organic and Biomolecular Chemistry
Uncontrolled Keywords:
?? spectrometry-mass spectrometrycytochrome-cfluorescent proteindesigned moleculesdrug discoveryrecognitionreceptorsbindingcomplexespeptidebiochemistryorganic chemistryphysical and theoretical chemistry ??
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Deposited On:
08 Jan 2015 09:00
Last Modified:
15 Jul 2024 14:58