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

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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Protein destabilisation by ruthenium(II) tris-bipyridine based protein-surface mimetics. / Wilson, Andrew J.; Ault, James R.; Filby, Maria H. et al.
In: Organic and Biomolecular Chemistry , Vol. 11, No. 13, 07.04.2013, p. 2206-2212.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Wilson, AJ, Ault, JR, Filby, MH, Philips, HIA, Ashcroft, AE & Fletcher, NC 2013, 'Protein destabilisation by ruthenium(II) tris-bipyridine based protein-surface mimetics', Organic and Biomolecular Chemistry , vol. 11, no. 13, pp. 2206-2212. https://doi.org/10.1039/c3ob26251k

APA

Wilson, A. J., Ault, J. R., Filby, M. H., Philips, H. I. A., Ashcroft, A. E., & Fletcher, N. C. (2013). Protein destabilisation by ruthenium(II) tris-bipyridine based protein-surface mimetics. Organic and Biomolecular Chemistry , 11(13), 2206-2212. https://doi.org/10.1039/c3ob26251k

Vancouver

Wilson AJ, Ault JR, Filby MH, Philips HIA, Ashcroft AE, Fletcher NC. Protein destabilisation by ruthenium(II) tris-bipyridine based protein-surface mimetics. Organic and Biomolecular Chemistry . 2013 Apr 7;11(13):2206-2212. doi: 10.1039/c3ob26251k

Author

Wilson, Andrew J. ; Ault, James R. ; Filby, Maria H. et al. / Protein destabilisation by ruthenium(II) tris-bipyridine based protein-surface mimetics. In: Organic and Biomolecular Chemistry . 2013 ; Vol. 11, No. 13. pp. 2206-2212.

Bibtex

@article{58c4153b706a4a24b4bc01af5e1f5f9a,
title = "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 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.",
keywords = "SPECTROMETRY-MASS SPECTROMETRY, CYTOCHROME-C, FLUORESCENT PROTEIN, DESIGNED MOLECULES, DRUG DISCOVERY, RECOGNITION, RECEPTORS, BINDING, COMPLEXES, PEPTIDE",
author = "Wilson, {Andrew J.} and Ault, {James R.} and Filby, {Maria H.} and Philips, {Hazel I. A.} and Ashcroft, {Alison E.} and Fletcher, {Nicholas C.}",
year = "2013",
month = apr,
day = "7",
doi = "10.1039/c3ob26251k",
language = "English",
volume = "11",
pages = "2206--2212",
journal = "Organic and Biomolecular Chemistry ",
issn = "1477-0520",
publisher = "Royal Society of Chemistry",
number = "13",

}

RIS

TY - JOUR

T1 - Protein destabilisation by ruthenium(II) tris-bipyridine based protein-surface mimetics

AU - Wilson, Andrew J.

AU - Ault, James R.

AU - Filby, Maria H.

AU - Philips, Hazel I. A.

AU - Ashcroft, Alison E.

AU - Fletcher, Nicholas C.

PY - 2013/4/7

Y1 - 2013/4/7

N2 - 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.

AB - 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.

KW - SPECTROMETRY-MASS SPECTROMETRY

KW - CYTOCHROME-C

KW - FLUORESCENT PROTEIN

KW - DESIGNED MOLECULES

KW - DRUG DISCOVERY

KW - RECOGNITION

KW - RECEPTORS

KW - BINDING

KW - COMPLEXES

KW - PEPTIDE

U2 - 10.1039/c3ob26251k

DO - 10.1039/c3ob26251k

M3 - Journal article

VL - 11

SP - 2206

EP - 2212

JO - Organic and Biomolecular Chemistry

JF - Organic and Biomolecular Chemistry

SN - 1477-0520

IS - 13

ER -