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Type: Journal article
Title: Reversible photoregulation of binding of α-chymotrypsin to a gold surface
Other Titles: Reversible photoregulation of binding of alpha-chymotrypsin to a gold surface
Author: Pearson, D.
Downard, A.
Muscroft-Taylor, A.
Abell, A.
Citation: Journal of the American Chemical Society, 2007; 129(48):14862-14863
Publisher: Amer Chemical Soc
Issue Date: 2007
ISSN: 0002-7863
Statement of
David Pearson, Alison J. Downard, Andrew Muscroft-Taylor, and Andrew D. Abell
Abstract: An ability to optically modulate the interactions of surfaces with functional biomolecules provides an important basis for generating new technologies including reversible biosensors, advanced medical implants, and biomolecular computers. Here we report the first example of reversible photoregulation of binding of a protease to a functional surface. A modular approach is presented with a surface-bound inhibitor containing a photoisomerizable azobenzene core to which is attached (i) appropriate protease binding functionality and (ii) a tether for surface attachment. The principle is demonstrated for alpha-chymotrypsin using a phenylalanine-based trifluoromethylketone inhibitor containing an azobenzene core and an alkyne-functionalized ethylene glycol tether, which is attached to the surface using click chemistry. UV/vis irradiation of the functional surface leads to a significant, reversible change in the amount of alpha-chymotrypsin that attaches to the surface, as measured by surface plasmon resonance.
Keywords: Gold
Protease Inhibitors
Surface Plasmon Resonance
Molecular Structure
Description: Copyright © 2007 American Chemical Society
DOI: 10.1021/ja0766674
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Appears in Collections:Aurora harvest
Chemistry publications

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