Systematic ways to generate high-affinity, high-selectivity and renewable binders of human proteins are reported online this week in Nature Methods. These results suggest that a large-scale effort to create renewable reagents to detect all human proteins should be feasible with existing methods and tools.
Antibodies are produced naturally as part of the immune system in animals. For decades, researchers have taken advantage of this process to create specific reagents that work in a similar fashion to antibodies, binding to proteins of interest. Such reagents are extremely important research tools, and are used extensively in the laboratory to detect or isolate a protein of interest from a biological sample. Although thousands of commercially available antibodies exist, their quality varies widely and most of these antibodies are not renewable ― their exact compositions differ from batch to batch.
Karen Colwill, Susanne Gräslund and collaborators report the results of a pilot project to evaluate the generation of several types of renewable antibody-like reagents to 20 closely related human proteins. They demonstrated that the renewable reagents could be efficiently produced within a reasonable time frame and had affinities and selectivities on par with traditional antibodies.