The authors developed mini-antibodies using software that predicts how
This is very amazing stuff! It opens up many possibilities.
Stephen Mayo, chemist at Caltech
Antibodies bind well to proteins, e.g.with different microbes. Therefore, pharmaceutical companies use them as drugs to fight infections and cancer. But antibodies are large proteins, so they are expensive to make and the process is often unstable. The study authors worked to overcome these problems.
The process by which antibodies bind to a targetlooks like a rock climber trying to climb a sheer cliff, explains David Baker, a computational structural biologist at the University of Washington (UW). The surface of such a rock is usually smooth, and there is little support for arms and legs. The antibodies are large, so they can make many grips at the same time and hold on firmly.
But mini-antibodies have fewer possibilities.The researchers tried to overcome this shortcoming; they identified the capture sites on the proteins and built mini-antibodies based on this. But this only works for well-studied proteins.
To get around this problem, Baker and colleaguesturned to the Rosetta software, which they developed to predict protein structures based on their amino acid sequence. To create a map of potential footholds, the team tasked the program with calculating how tightly defined amino acids would bind to various points on the target protein's surface. The researchers used Rosetta to create tens of thousands of virtual mini-antibodies.
This software will allowresearchers to develop diagnostic probes to help detect diseases at an early stage, adds Tanya Kortemme, a bioengineer at the University of California, San Francisco.
We can design proteins tocontact any target. This means that miniproteins can not only block disease-causing proteins, but also direct drugs to cancerous tissues or deliver light-emitting or radioactive diagnostic molecules to any cells. This will help track progress in treatment.
Longxin Cao, UW postdoc
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