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. 2010 May 10;10(5):4739–4755. doi: 10.3390/s100504739

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© 2010 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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Figure 1. — (A) SEM image of organic SLP biosensor layer bound to a gold working electrode. Dense protein layer covalently bound with boundaries between protein domains. (B) XPS analysis of surface composition of top 5nm of bound protein layer before ( ) and after ( ) chemical modification of phosphate and carboxylate groups. The data show a 30.2% carbon C 1s to gold 4f peak ratio increase confirming successful modification of analyte binding sites.

Inline graphic — (A) SEM image of organic SLP biosensor layer bound to a gold working electrode. Dense protein layer covalently bound with boundaries between protein domains. (B) XPS analysis of surface composition of top 5nm of bound protein layer before ( ) and after ( ) chemical modification of phosphate and carboxylate groups. The data show a 30.2% carbon C 1s to gold 4f peak ratio increase confirming successful modification of analyte binding sites.