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J Am Chem Soc. 2009 Dec 30;131(51):18202-3. doi: 10.1021/ja907066r.

Identifying modulators of protein-protein interactions using photonic crystal biosensors.

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  • 1Department of Biochemistry, University of Illinois, Urbana, Illinois 61801, USA.


Inhibitors and activators of protein-protein interactions are valuable as biological probes and medicinal agents but are often difficult to identify. Herein we describe a high-throughput assay, based upon photonic crystal (PC) biosensors, for the identification of modulators of protein-protein interactions. Through the use of a d-biotin-tris-NTA (BTN) hybrid compound, any His6-tagged protein can be immobilized on the surface of a PC biosensor. Binding of the bound protein to its cognate partner is detected via a shift in the peak wavelength value. We demonstrate this assay with three protein-protein pairs (caspase-9-XIAP, caspase-7-XIAP, FKBP12-FRB) and their small molecule modulators.

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