Method for covalent cross-linking of antibodies to surfaces for immunoassays and targeted drug delivery
The Tsourkas Lab has designed a facile method for the site-specific bioconjugation of native immunoglobulins (IgGs). The researchers have developed novel photoreactive Protein Z variants that allow for the introduction of a diverse range of modifications, including azides, haptens, and fluorophores, onto IgG. The Protein Z variants can be expressed recombinantly at a high yield in E. coli, with incorporation of the non-natural amino acid benzoylphenylalanine and C-terminal modifications.
The variants can be rapidly cross-linked to many types of IgG, including human, mouse, and rabbit, with efficiency up to 95% after 1 hour of UV exposure. This efficient, site-specific conjugation system allows for a cost-effective method to functionalize antibodies.
Andrew Tsourkas, Professor, Department of Bioengineering
- Robust, high-yield, cost-effective system
- Fast kinetics, site-specific labeling
- Diverse range of C-terminal modifications
- Long wavelength UV light does not damage protein
- Compatible with most native IgGs
Stage of Development:
Proof of principle and in vitro testing
UP application (PCT/US2014/030457)
Hui JZ et al. Bioconjugate Chemistry, 2014, 25(9), 1709-1719.
Docket # Z6629