Issue 20, 2013

Gold nanoparticle-linked analysis of carbohydrate–protein interactions, and polymeric inhibitors, using unlabelled proteins; easy measurements using a ‘simple’ digital camera

Abstract

Traditional methods of measuring the affinity of lectins (or other carbohydrate-binding proteins) to their target carbohydrate ligand rely on the use of chemically/recombinantly modified proteins in sorbent assays, microarrays or the use of expensive label-free methods such as surface plasmon resonance spectrometry. In this work we exploit the extremely high extinction coefficient (i.e. colour) of gold nanoparticles as resolving agents in sorbent assays. The anionic nanoparticles adhere strongly to immobilized proteins, but not to the carbohydrate-surfaces allowing investigation of protein binding and screening of novel multivalent inhibitors. Furthermore, the use of a simple digital camera (or mobile phone) to obtain the data is shown, providing a simple ultra-low cost route to the detection of unmodified, carbohydrate-binding proteins.

Graphical abstract: Gold nanoparticle-linked analysis of carbohydrate–protein interactions, and polymeric inhibitors, using unlabelled proteins; easy measurements using a ‘simple’ digital camera

Supplementary files

Article information

Article type
Paper
Submitted
21 Feb 2013
Accepted
10 Apr 2013
First published
10 Apr 2013

J. Mater. Chem. B, 2013,1, 2665-2672

Gold nanoparticle-linked analysis of carbohydrate–protein interactions, and polymeric inhibitors, using unlabelled proteins; easy measurements using a ‘simple’ digital camera

L. Otten, S. Richards, E. Fullam, G. S. Besra and M. I. Gibson, J. Mater. Chem. B, 2013, 1, 2665 DOI: 10.1039/C3TB20259C

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