Antibody purification via affinity chromatography that utilizes the nucleotide binding site
Tech ID: 11-025
Inventors: Zihni Basar Bilgicer, Tanyel Kiziltepe-Bilgicer, Nathan J. Alves, Jonathan Darryl Ashley, Michael William Handlogten
Overview
A novel, inexpensive antibody purification method with enhanced stability and higher specificity.
Technology Summary
Current antibody purification methods have a short lifetime, contaminate the antibody due to leaching, decreases antibody activity due to denaturation or aggregation, and possess steric constraints leading to lower column capacity. Other alternatives are either more expensive, or do not offer enough specificity to be successful in the market.
This technology solves the problem of expensive purification methods in the production of antibodies. In addition, it also provides better results than current purification methods.
The Notre Dame Research Team has developed a novel method that uses indole butyric acid (IBA) attached to a Toyo Pearl resin to selectively target antibodies at their conserved Nucleotide Binding Site (NBS). Toyo Pearl is a commercially available polymer-resin, which was chosen due to its optimal characteristics for small-molecule-based affinity chromatography. The Toyo Pearl makes up the stationary phase component of the affinity chromatography column. Coupled to the resin is the indole butyric acid (IBA), which is a specific compound that has a monovalent affinity for the nucleotide binding site. The advantage of NBS is that, it is present across various antibody species and all antibody isotypes.
Market Advantages
- Lowers antibody purification costs
- Provides higher Amount of Antibody Recover >95%
- Highly pure. Purity>98%
Technology Readiness Level
TRL 4 - Lab Validation
Seeking
Licensing and Research Collaboration
Publication
https://doi.org/10.1021/ac300952r
Intellectual Property
US pat. no. 9,598,460
Contact
Richard Cox
rcox4@nd.edu
574.631.5158