VATIS UPDATE Article

Scientists from the University of Washington (UW), the United States, have created a high-speed method to generate thousands of different, small, stable proteins from scratch that can be custom-designed to bind to specific therapeutic targets. The method used a computer platform, called Rosetta, developed by Baker and colleagues at UW. They designed thousands of short proteins, about 40 amino acids in length that the Rosetta program predicted would bind tightly to the molecular target.

Due to their small size, these short proteins tend to be extremely stable. They can be stored without refrigeration. They also are more easily administered than large protein drugs, such as monoclonal antibodies. Previously, such short, protein-binder drugs were typically re-engineered versions of naturally occurring proteins. These, however, tended not to be significantly better than monoclonal antibodies.

Because these mini-proteins binders are original designs, they can be tailored to fit their targets much more tightly and are simpler to modify and refine. In this study, the researchers sought to design two sets of these proteins: one set that would prevent the influenza virus from invading cells and another that would bind to and neutralize a deadly nerve toxin from botulism. This toxin is considered a potential bioweapon.