Researchers at the Biodesign Institute at Arizona State University have found a way to get molecular binding agents to act like antibodies and, in the process, optimize the binding agents’ affinity for targeted proteins. The development revealed important nuances of protein function and could lead to better diagnosis and treatment for a range of diseases. The researchers published their findings Aug. 16 in the journal ChemBioChem.
It also demonstrated the feasibility of producing antibodies suitable for research in a less costly and labor-intensive way than previously shown.
Traditionally, antibodies for research have been extracted from animals induced to produce them in response to various protein antigens, according to a statement from Arizona State. While the technique has been invaluable to medical science, obtaining antibodies in this way “is a cumbersome and costly endeavor.”
Instead, Chaput and his team produce synthetic antibodies that do not require cell culture, in vitro selection or the application of complex chemistry. They call their reagents DNA synbodies.
“This dramatic change in affinity has the ability to transform ordinary molecules into a high affinity synthetic antibody,” explained researcher John Chaput, PhD, of the department of chemistry and biochemistry at Arizona State. “Unfortunately, the chemistry used to make these reagents can be quite challenging and often requires a lot of trial and error. With NIH funding, my group has reduced the complexity of this problem to simple chemistry that is user friendly and easily amenable to high throughput automation.”
The new technique is referred to as LINC, for Ligand Interaction by Nucleotide Conjugates.