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Issue 19, 2007
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Site-specific protein immobilization through N-terminal oxime linkages

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Immobilizing proteins in specific orientations is important for diagnostic protein arrays, biomaterials, and other applications where retention of bioactivity is essential. We report an approach for protein micropatterning that exploits a chemoselective reaction to conjugate proteins at the N-terminus to polymer films. A copolymer from 2-hydroxyethyl methacrylate and a Boc-protected aminooxy tetra(ethylene glycol) methacrylate was synthesized by radical polymerization. Boc groups were locally deprotected using photoacid generator-based photolithography. Micropatterns were verified by fluorescence microscopy utilizing green fluorescent aldehyde microspheres. Streptavidin that was subjected to a transamination reaction to install an α-ketoamide group at the N-terminus was conjugated to the patterns by oxime bond formation. Since the majority of proteins may be modified to contain a reactive carbonyl group, this methodology should be applicable to pattern a wide variety of proteins specifically through the N-terminus.

Graphical abstract: Site-specific protein immobilization through N-terminal oxime linkages

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Article information

11 Dec 2006
01 Mar 2007
First published
14 Mar 2007

J. Mater. Chem., 2007,17, 2021-2027
Article type

Site-specific protein immobilization through N-terminal oxime linkages

K. L. Christman, R. M. Broyer, Z. P. Tolstyka and H. D. Maynard, J. Mater. Chem., 2007, 17, 2021
DOI: 10.1039/B618002G

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