Researchers at Duke University School of Medicine developed an artificial-intelligence framework called Raygun that can redesign existing proteins [1].

This capability allows scientists to modify the size of proteins without sacrificing their biological function. By enabling precise edits that mimic evolutionary processes, the tool could accelerate the development of new medicines and industrial enzymes [2].

The Raygun system operates by adding, deleting, or substituting amino-acid subunits within a protein's structure [1, 3]. This allows proteins to be shrunk or supersized while maintaining the specific shape, and chemical properties required for them to work [1, 3].

Protein engineering has traditionally been a slow process, often relying on trial and error or limited natural mutations. The new AI framework aims to make this process faster and more predictable by strategically identifying which parts of a protein can be removed or altered without causing the entire structure to collapse [2].

Based in North Carolina, the Duke University team designed the system to handle the complex geometry of proteins [1]. The tool can suggest specific modifications to the amino-acid sequence to achieve a desired size change while preserving the protein's active site, the area where the protein interacts with other molecules [2].

Because the system can both shrink and enlarge proteins, it provides a flexible toolkit for researchers across various scientific disciplines [3]. The ability to reduce the size of a protein may be particularly useful for creating more stable drugs that can more easily enter cells or cross biological barriers [2].

“Raygun can redesign existing proteins by adding, deleting, or substituting amino-acid subunits.”

The ability to precisely resize proteins without destroying their utility represents a shift from discovering proteins to designing them. By reducing the physical footprint of a protein while keeping its function intact, researchers may overcome significant delivery hurdles in pharmacology, potentially leading to smaller, more efficient therapeutic proteins that are easier for the human body to absorb.