Metal complexes as "protein surface mimetics"

Sarah H. Hewitt, Andrew J. Wilson*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

22 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)9745-9756
Number of pages12
JournalChemical Communications
Volume52
Issue number63
DOIs
Publication statusPublished - 2016

Bibliographical note

Funding Information:
This work was supported by the Engineering and Physical Sciences Research Council [EP/L504993/1, EP/F039069 and EP/F038712] and by the European Research Council [ERC-StG-240324]

Publisher Copyright:
© The 2016 The Royal Society of Chemistry.

ASJC Scopus subject areas

  • Catalysis
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • General Chemistry
  • Surfaces, Coatings and Films
  • Metals and Alloys
  • Materials Chemistry

Fingerprint

Dive into the research topics of 'Metal complexes as "protein surface mimetics"'. Together they form a unique fingerprint.

Cite this