Key proteins contribute to the treatment of muscular dystrophy

Recently, researchers from the University of Alberta have identified potential targets for the treatment of Lou Grieg's disease, a neuromuscular degeneration   Biophysicist Michael Woodside first observed the folding process of SOD1 (superoxide dismutase, an antioxidant whose wrong folding can lead to neuromuscular degeneration) by using single molecule technology, and they found that this process is much more complicated than previously thought   These results explain the preference of protein misfolding, which is similar to prion   "When we separate proteins, we want them to maintain their original structure, as we thought before, but in fact, we find that proteins have become a mess," said Woodside, a professor from the Department of physics at the University of Alberta "But after thousands of times of unfolding and refolding, we find that they can show more clear characteristics." we We can have a clearer understanding of the structure of the protein from the level of single molecule, so that the whole structure of the protein can be completely spliced   Professor Woodside is best known for his work on the structure of prions such as mad cow disease According to Professor Woodside, the misfolded properties of SOD1 are very similar to prion proteins Using optical tweezers, the process of SOD1 was studied in detail Woodside explained that the protein has a stable core, which is always the last to fold and the first to fold   The author and others finally found that the root cause of the whole protein folding is the wrong folding of the core They found some wrong folding methods, and solved the complex folding intermediate structure which had not been detected before, making the whole folding process more clear   Based on this result, the author and others hope to further expand the discovery, that is, to combine single molecules with the whole cell, even the whole life Now he is working with doctors in ALS to find out the protein misfolding process that leads to ALS   The results were published in the latest issue of nature communications.