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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
 

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.

 

Inventor:

Andrew Tsourkas, Professor, Department of Bioengineering 

 

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

Docket # Z6629

 

 

Download PDF

 


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