Enhanced electrostatic discrimination of proteins on nanoparticle-coated surfaces

Xu, Y. S. and Engel, Y. and Yan, Y. F. and Chen, K. M. and Moyano, D. F. and Dubin, P. L. and Rotello, V. M.. (2013) Enhanced electrostatic discrimination of proteins on nanoparticle-coated surfaces. Journal of Materials Chemistry B, 1 (39). pp. 5230-5234.

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Two beta-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.

Item Type: Article
Additional Information: ISI Document Delivery No.: 221TLTimes Cited: 0Cited Reference Count: 22Xu, Yisheng Engel, Yoni Yan, Yunfeng Chen, Kaimin Moyano, Daniel F. Dubin, Paul L. Rotello, Vincent M.NIH GM077173; Center for Hierarchical Manufacturing CMMI-1025020This work was supported by the NIH (GM077173) and the Center for Hierarchical Manufacturing (CMMI-1025020). We thank Prof. Robert Weis for access to the SPR instrument, Prof. Greg Grason for helpful discussions on monolayer electrostatics.Royal soc chemistryCambridge
Uncontrolled Keywords: ph
Collections: Nanomanufacturing Research Collection > Nanomanufacturing Nanoscale Science and Engineering Centers > Center for Hierarchical Manufacturing
Depositing User: Robert Stevens
Date Deposited: 27 Mar 2014
Last Modified: 27 Mar 2014 20:21
URI: http://eprints.internano.org/id/eprint/2163

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