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Site-specific bioconjugation of native immunoglobulins

Description:

Method for covalent cross-linking of antibodies to surfaces for immunoassays and targeted drug delivery

 

Inventor

Andrew Tsourkas, Professor, Department of Bioengineering 

 

 

Technology Overview

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.

 

Advantages

• 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 

Intellectual Property

UP application (PCT/US2014/030457)

 

Reference Media

Hui JZ et al.  Bioconjugate Chemistry, 2014, 25(9), 1709-1719.

 

Desired partnerships

•  License

Co-development

 

 

Download PDF

 

Docket #  Z6629 


Patent Information:
For Information, Contact:
Joshua Jeanson
Associate Director, SEAS/SAS Licensing Group
University of Pennsylvania
jeanson@upenn.edu
Inventors:
Andrew Tsourkas
Keywords:
Biotechnology
Engineering