Specific Covalent Immobilization of Proteins through Dityrosine Crosslinks: New Chemistry to Improve Protein Arrays

This invention provides a new immobilization chemistry that combines the versatility of specific protein immobilization with the advantages of site-specific covalent crosslinking. Target proteins are first reversibly surface associated through the well-known interaction of His6-peptide tags and NTA-Ni(II) complexes. Upon addition of an oxidant, a co-localized peptide-Ni(II) complex catalyzes covalent crosslinking between tyrosine residues strategically placed adjacent to the His6 peptide tag and the catalytic peptide complex.

This unique metal-catalyzed crosslinking system is applicable in the area of specific and oriented immobilization of proteins. Specific applications include protein arrays for clinical diagnostics and proteomics research, protein-based biosensors, and immobilization of enzymes used in industrial processing.

Stage of Development
The international patent application PCT/US04/25958 has been filed on this technology. This invention is available under any sort of licensing or sponsored research arrangement.

Additional Info
*Stayner RS, Min DJ, Kiser PF, Stewart RJ. (Nov-Dec 2005 ) �Site-specific cross-linking of proteins through tyrosine hexahistidine tags� Bioconjug Chem. 16(6):1617-23

Inventor(s): Patrick Kiser, Cynthia Burrows, Ann Stemmler, Richard Scott Stayner, Dong-Joon Min, Russell Stewart

Type of Offer: Licensing

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