Self-assembled protein2018-11-13 00:25:40 224 ℃
Helps to synthesize new materials that do not exist in nature
Technology Daily, Beijing, November 11 (Reporter Liu Xia) According to a recent report by the American Physicist Organization Network, American scientists have started from scratch for the first time. And manufacture self-assembled protein filaments. These protein filaments are long helical linear structures formed by the spontaneous binding of the same protein subunits. The latest research will help scientists better understand the structural and mechanical properties of natural protein filaments and create new materials that do not exist in nature, including man-made fibers that rival or exceed the strength of spider silk, as well as nanoscale circuits.
In nature, protein filaments are an essential component of several structural and motor parts of living cells and many body tissues. These structures and tissues include the cytoskeleton that allows cells to form specific structures, the microtubules that coordinate cell division, and the most common protein in our body, collagen.
To design this new protein, the team led by David Baker, a professor of biochemistry at the University of Washington School of Medicine, used a computer program called "Rosetta" developed by Baker Labs. The program can predict its shape by the amino acid sequence of the protein. They used Rosetta to design a small protein with amino acids on the surface that allowed them to lock into each other and self-assemble into spiral protein filaments. The researchers said that with this method, "we can finally design a protein that can be assembled like Lego bricks." The results have been published online in the journal Science.
The first author of the paper, George Fallas, a lecturer at the University of Washington School of Medicine, said that the new method designed a relatively small protein consisting of only 180 to 200 amino acids and only about 1 nanometer in length. However, it can be assembled into stable filaments with a length of over 10,000 nm.
The study also demonstrated that filament growth or dissociation can be driven by modifying the concentration of the designed protein in solution and adding an additive that inhibits protein binding.
Baker said: "The ability to program filament formation power will give us insight into how protein filaments in nature are assembled and unraveled. These proteins are very stable and can be used as easy-to-modify stents. From new diagnostic tests to nanoelectronics and other fields."
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