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Issue 2, 2012
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A methodology for preparing nanostructured biomolecular interfaces with high enzymatic activity

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Abstract

The development of a novel method for functionalizing nanopatterned surfaces with catalytically active proteins is reported. This method involves using dip-pen nanolithography (DPN) and polymer pen lithography (PPL) to generate nanoscale patterns of coenzyme A, followed by a phosphopantetheinyl transferase-mediated coupling between coenzyme A and proteins fused to the ybbR-tag. By exploiting the ability to generate protein features over large areas afforded by DPN and PPL, it was now possible to measure protein activity directly on these surfaces. It was found that proteins immobilized on the nanoscale features not only display higher activity per area with decreasing feature size, but are also robust and can be used for repeated catalytic cycles. The immobilization method is applicable to a variety of proteins and gives rise to superior activity compared to proteins attached in random orientations on the surface.

Graphical abstract: A methodology for preparing nanostructured biomolecular interfaces with high enzymatic activity

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Publication details

The article was received on 04 Oct 2011, accepted on 02 Nov 2011 and first published on 08 Dec 2011


Article type: Paper
DOI: 10.1039/C1NR11443C
Citation: Nanoscale, 2012,4, 659-666
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    A methodology for preparing nanostructured biomolecular interfaces with high enzymatic activity

    L. S. Wong, C. V. Karthikeyan, D. J. Eichelsdoerfer, J. Micklefield and C. A. Mirkin, Nanoscale, 2012, 4, 659
    DOI: 10.1039/C1NR11443C

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