SATURDAY, OCTOBER 1, 2016

Improved methods for engineering therapeutic proteins into antibodies

Improved methods for engineering therapeutic proteins into antibodies | Courtesy of biology.usf.edu
A team of researchers from The Scripps Research Institute (TSRI) recently created a better way to engineer therapeutic proteins in antibodies, which would allow antibodies to persist against invading bacteria and viruses for longer periods of time.

Some proteins do not exist for long periods of time within the bloodstream. This means that these proteins are not effective for therapies, but scientists can build these into larger proteins, like antibodies, which will allow them to last longer and help the body’s immune response.

The new method creates millions of potential junction segments between the antibody host and the inserted protein. Designers chose the rare proteins that would fold and function normally with the inserted protein.

This technique will allow for new diagnostic and drug compounds, like hormone-based therapies.

“Unlike prior approaches to this design problem, ours is a selection-based method—and it’s hard to beat this approach, with its ability to harness the power of very large numbers,” Richard A. Lerner, senior investigator and the Lita Annenberg Hazen Professor of Immunochemistry at TSRI, said.

With this new process, essentially a measuring device is placed in the middle of the protein to determine if it's folded correctly, Lerner said.

“The kidneys and other organs clear it very rapidly,” Yingjie Peng, a staff scientist in the Lerner laboratory who was first author of the study with Wenwen Zeng of Friedman’s lab at Rockefeller, said. “But it could last much longer if it were part of a larger structure such as an antibody.”

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