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Abstract
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 language | English |
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Pages (from-to) | 2206-2212 |
Number of pages | 7 |
Journal | Organic and Biomolecular Chemistry |
Volume | 11 |
Issue number | 13 |
Early online date | 30 Jan 2013 |
DOIs | |
Publication status | Published - 2013 |
ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Organic Chemistry
- Biochemistry
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Dive into the research topics of 'Protein destabilisation by ruthenium(II) tris-bipyridine based protein-surface mimetics'. Together they form a unique fingerprint.Projects
- 1 Finished
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R1928CHM: Metal complexes as Inhibitors of Protein-Protein interactions
Fletcher, N. (PI)
01/08/2007 → 31/03/2011
Project: Research