Monitoring the activity of tyrosinase on a tyramine/dopamine-functionalized surface by force microscopy

Adam B. Braunschweig; Roey Elnathan; Itamar Willner

doi:10.1021/nl0708819

Monitoring the activity of tyrosinase on a tyramine/dopamine-functionalized surface by force microscopy

Adam B. Braunschweig, Roey Elnathan, Itamar Willner

Research output: Contribution to journal › Article › Research › peer-review

11 Citations (Scopus)

Abstract

Tyrosinase activity is monitored by π-donor-acceptor force interactions between a bipyridinium-modified AFM tip and the biocatalytic reaction product generated on a tyramine- (or dopamine-) modified surface. Upon oxidation of the surface to dopaquinone as a result of tyrosinase activity, force interactions are switched "OFF". After reduction of the resulting surface with ascorbic acid, forces are quantitatively reestablished as a result of the formation of the dopamine-functionalized surfaces. The method provides a general approach to design biosensors using force interactions as the readout signal.

Original language	English
Pages (from-to)	2030-2036
Number of pages	7
Journal	Nano Letters
Volume	7
Issue number	7
DOIs	https://doi.org/10.1021/nl0708819
Publication status	Published - 1 Jul 2007
Externally published	Yes

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AB - Tyrosinase activity is monitored by π-donor-acceptor force interactions between a bipyridinium-modified AFM tip and the biocatalytic reaction product generated on a tyramine- (or dopamine-) modified surface. Upon oxidation of the surface to dopaquinone as a result of tyrosinase activity, force interactions are switched "OFF". After reduction of the resulting surface with ascorbic acid, forces are quantitatively reestablished as a result of the formation of the dopamine-functionalized surfaces. The method provides a general approach to design biosensors using force interactions as the readout signal.

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Monitoring the activity of tyrosinase on a tyramine/dopamine-functionalized surface by force microscopy

Abstract

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