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


ABSTRACT: 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.

SUBMITTER: Heeres JT 

PROVIDER: S-EPMC2799191 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature

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

Heeres James T JT   Kim Seok-Ho SH   Leslie Benjamin J BJ   Lidstone Erich A EA   Cunningham Brian T BT   Hergenrother Paul J PJ  

Journal of the American Chemical Society 20091201 51


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  ...[more]

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