Research Corporation Technologies (RCT) is tapping Isogenica for use of the latter’s CIS display platform to screen its antibody-derived engineered CH2 domain libraries. The libraries are the foundation of a biologics discovery platform centered on the discovery of therapeutic antibody-derived Abdurin™ molecules, which the firm is offering through drug discovery partnerships. Developed in collaboration with scientists at the Protein Interactions Group of the National Cancer Institute, the antigen-specific Abdurins retain the long half-life of an antibody’s CH2 domain, and can be engineered to demonstrate enhanced stability and epitope binding.

RCT claims that Isogenica’s CIS display platform can screen much larger libraries and isolate and optimize lead bindings much faster than phage display approaches. Through the partnership Isogenica will also support RCT through deep sequencing and related bioinformatics tools to help optimize selected abdurins against specific targets.

“Isogenica’s CIS display offers a significant advantage over other screening systems by allowing for primary screening and binder optimization in one system,” comments Kurt Gehlsen, Ph.D., vp and CSO at RCT. “The pairing of CIS display with our Abdurins platform will be an attractive offering to potential partners.”

RCT is a technology investment and management company that provides early-stage funding and development for promising biomedical companies and technologies. The firm separately reported the publication of the first studies in primates to characterize the long half-life of isolated CH2 domain scaffold. The work was performed under a Cooperative Research and Development Agreement (CRADA) between RCT and the NI, in collaboration with the NCI’s Protein Interactions Group. The firm says the data represent the first to demonstrate that a small protein scaffold can retain an extended half-life in nonhuman primates without modifications such as pegylation.

“We believe that our Abdurins platform addresses several of the known shortcomings of other small antibody-like fragments through its longer half-life, ease of production, and flexible formatting,” adds Shaun Kirkpatrick, president and CEO at RCT. “We are looking forward to partnering with industry and developing the next generation of antibody-like therapeutics.”

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