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  Patterned biofunctional poly(acrylic acid) brushes on silicon surfaces.

Dong, R., Krishnan, S., Baird, B. A., Lindau, M., & Ober, C. K. (2007). Patterned biofunctional poly(acrylic acid) brushes on silicon surfaces. Biomakromolecules, 8(10), 3082-3092. doi:10.1021/bm700493v.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-A930-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C616-6
Genre: Journal Article

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2166931.pdf (Publisher version), 475KB
 
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http://pubs.acs.org/doi/pdf/10.1021/bm700493v (Publisher version)
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 Creators:
Dong , R., Author
Krishnan, S., Author
Baird , B. A., Author
Lindau, M.1, Author              
Ober , C. K., Author
Affiliations:
1Research Group of Nanoscale Cell Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1832294              

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 Abstract: Protein patterning was carried out using a simple procedure based on photolithography wherein the protein was not subjected to UV irradiation and high temperatures or contacted with denaturing solvents or strongly acidic or basic solutions. Self-assembled monolayers of poly(ethylene glycol) (PEG) on silicon surfaces were exposed to oxygen plasma through a patterned photoresist. The etched regions were back-filled with an initiator for surface-initiated atom transfer radical polymerization (ATRP). ATRP of sodium acrylate was readily achieved at room temperature in an aqueous medium. Protonation of the polymer resulted in patterned poly(acrylic acid) (PAA) brushes. A variety of biomolecules containing amino groups could be covalently tethered to the dense carboxyl groups of the brush, under relatively mild conditions. The PEG regions surrounding the PAA brush greatly reduced nonspecific adsorption. Avidin was covalently attached to PAA brushes, and biotin-tagged proteins could be immobilized through avidin-biotin interaction. Such an immobilization method, which is based on specific interactions, is expected to better retain protein functionality than direct covalent binding. Using biotin-tagged bovine serum albumin (BSA) as a model, a simple strategy was developed for immobilization of small biological molecules using BSA as linkages, while BSA can simultaneously block nonspecific interactions.

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Language(s): eng - English
 Dates: 2007-09-202007-10
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1021/bm700493v
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Title: Biomakromolecules
Source Genre: Journal
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Pages: - Volume / Issue: 8 (10) Sequence Number: - Start / End Page: 3082 - 3092 Identifier: -