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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]

PMID: 19968284

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