Issue 13, 2013

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.

Graphical abstract: Protein destabilisation by ruthenium(ii) tris-bipyridine based protein-surface mimetics

Supplementary files

Article information

Article type
Paper
Submitted
01 ก.ค. 2555
Accepted
29 ม.ค. 2556
First published
30 ม.ค. 2556
This article is Open Access

Org. Biomol. Chem., 2013,11, 2206-2212

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

A. J. Wilson, J. R. Ault, M. H. Filby, H. I. A. Philips, A. E. Ashcroft and N. C. Fletcher, Org. Biomol. Chem., 2013, 11, 2206 DOI: 10.1039/C3OB26251K

This is an Open Access article. The full version of this article can be posted on a website/blog, posted on an intranet, photocopied, emailed, distributed in a course pack or distributed in Continuing Medical Education (CME) materials provided that it is not used for commercial purposes.

To request permission to reproduce material from this article in a commercial publication, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party commercial publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements