Hewitt, SH and Wilson, AJ (2016) Metal complexes as "protein surface mimetics". Chemical Communications, 52 (63). pp. 9745-9756. ISSN 1359-7345
Abstract
A key challenge in chemical biology is to identify small molecule regulators for every single protein. However, protein surfaces are notoriously difficult to recognise with synthetic molecules, often having large flat surfaces that are poorly matched to traditional small molecules. In the surface mimetic approach, a supramolecular scaffold is used to project recognition groups in such a manner as to make multivalent non-covalent contacts over a large area of protein surface. Metal based supramolecular scaffolds offer unique advantages over conventional organic molecules for protein binding, including greater stereochemical and geometrical diversity conferred through the metal centre and the potential for direct assessment of binding properties and even visualisation in cells without recourse to further functionalisation. This feature article will highlight the current state of the art in protein surface recognition using metal complexes as surface mimetics.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | © 2016, The Royal Society of Chemistry. This is an author produced version of a paper published in Chemical Communications. Uploaded in accordance with the publisher's self-archiving policy. |
Dates: |
|
Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Chemistry (Leeds) > Organic Chemistry (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 26 Jul 2016 10:24 |
Last Modified: | 18 Jul 2017 05:25 |
Published Version: | http://dx.doi.org/10.1039/C6CC03457H |
Status: | Published |
Publisher: | Royal Society of Chemistry |
Identification Number: | 10.1039/C6CC03457H |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:102817 |