Issue 39, 2013

Enhanced electrostatic discrimination of proteins on nanoparticle-coated surfaces

Abstract

Two β-lactoglobulin (BLG) isoforms, BLGA and BLGB, were used as a test bed for the differentiation of proteins using electrostatics. In these studies, the BLGA and BLGB binding to a highly charged, cationic gold nanoparticle (GNP) modified surface was investigated by atomic force microscopy (AFM) and surface plasmon resonance (SPR) spectroscopy. The binding affinity, and more importantly, the selectivity of this surface towards these two almost identical protein isoforms were both significantly increased on the cationic GNP surface array relative to the values measured with the same free cationic GNP in solution. While protein recognition is traditionally achieved almost exclusively via orientation dependent short-range interactions such as hydrogen bonds and hydrophobic interactions, our results show the potential of protein recognition platforms based on enhanced electrostatic interactions.

Graphical abstract: Enhanced electrostatic discrimination of proteins on nanoparticle-coated surfaces

Supplementary files

Article information

Article type
Paper
Submitted
18 mar. 2013
Accepted
30 abr. 2013
First published
30 abr. 2013

J. Mater. Chem. B, 2013,1, 5230-5234

Enhanced electrostatic discrimination of proteins on nanoparticle-coated surfaces

Y. Xu, Y. Engel, Y. Yan, K. Chen, D. F. Moyano, P. L. Dubin and V. M. Rotello, J. Mater. Chem. B, 2013, 1, 5230 DOI: 10.1039/C3TB20377H

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