Electrochemically Controllable Conjugation of Proteins on Surfaces

Mendes, Paula M. and Christman, Karen L. and Parthasarathy, Puru and Schopf, Eric and Ouyang, Jianyong and Yang, Yang and Preece, Jon A. and Maynard, Heather D. and Chen, Yong and Stoddart, J. Fraser. (2007) Electrochemically Controllable Conjugation of Proteins on Surfaces. Bioconjugate Chemistry, 18 (6). pp. 1919-1923. ISSN 1043-1802

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The rational design of surfaces for immobilization of proteins is essential to a variety of biological and medical applications ranging from molecular diagnostics to advanced platforms for fundamental studies of molecular and cell biology. We have developed an advanced electrochemically based approach for site-selective and reaction-controlled immobilization of proteins on surfaces. When a molecular monolayer of 4-nitrothiophenol on gold electrode surfaces is reduced electrochemically in a selective fashion at its nitro groups, to afford amino groups by potentiometric scans, the amine can be employed to orchestrate the immobilization of proteins to the surface. This protein immobilization strategy could allow one to fabricate intricate protein structures on surfaces for addressing fundamental and applied problems in biology and medicine.

Item Type: Article
Additional Information: Reprinted with permission from "Electrochemically Controllable Conjugation of Proteins on Surfaces", Mendes PM et al., Bioconjugate Chem., 2007, 18 (6), pp 1919–1923. Copyright 2007 American Chemical Society.
InterNano Taxonomy: Nanomanufacturing Processes > Self Assembly > Chemical surface functionalization
Nanomanufacturing Processes > Biological Techniques > Protein assembly
Nanoscale Objects and Nanostructured Materials > Other Nanostructured Materials > Self assembled monolayers
Collections: Nanomanufacturing Research Collection > Nanomanufacturing Nanoscale Science and Engineering Centers > Center for Scalable and Integrated Nanomanufacturing
Depositing User: Moureen Kemei
Date Deposited: 05 Apr 2010 14:54
Last Modified: 26 Sep 2014 21:18
URI: http://eprints.internano.org/id/eprint/403

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