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Issue 20, 2013
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Gold nanoparticle-linked analysis of carbohydrate–protein interactions, and polymeric inhibitors, using unlabelled proteins; easy measurements using a ‘simple’ digital camera

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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

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Publication details

The article was received on 21 Feb 2013, accepted on 10 Apr 2013 and first published on 10 Apr 2013


Article type: Paper
DOI: 10.1039/C3TB20259C
J. Mater. Chem. B, 2013,1, 2665-2672

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    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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