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


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 °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.

SUBMITTER: Wilson AJ 

PROVIDER: S-EPMC3731202 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature

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

Wilson Andrew J AJ   Ault James R JR   Filby Maria H MH   Philips Hazel I A HI   Ashcroft Alison E AE   Fletcher Nicholas C NC  

Organic & biomolecular chemistry 20130401 13


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  ...[more]

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