Walk to treat Alzheimer's. Scientists create an artificial piece of "Tao" protein

Santa Barbara, the American, has developed a team of scientists at the universities of the North Western and California, the first artificial piece of “Tao” protein that works in a similar way to the baronate, which is known for their ability to transfer their wrong forms to natural proteins, leading to their condensing way. The new “mini game” consists of a short part of the “Tao” protein, which involves a unique ability; It folds itself in the wrong way, collects in accurate strands that look like fibers and transfer this distortion to other healthy proteins, just like traditional bronze. The distorted protein similar to windshield wipers is the most important driving force for the development of a group of neurological degenerative diseases, the most important of which is Alzheimer’s disease. These diseases are characterized by abnormal accumulation of deformed tau protein in the brain, which leads to the weakening of nerve functions. According to the researchers, the development of a miniature artificial version of the entire human “Tao” protein opens the door to design more specific and effective diagnostic and therapeutic instruments for these diseases that have long expanded on modern medicine. Scientists have also discovered a hidden but important role for protein water. It appears that a common genetic mutation is usually used in the modeling of neurological degeneration diseases, the structure of water around the protein has changed slightly, which contributes to being pushed to structural distortion. The study, which will be published in the Journal of the National Academy of Sciences, reveals that the arrangement of variable water molecules contributes to the stabilization of proteins as a result of mutation, which helps build pathological fibers that characterize these neurological disorders. It is advanced to understand complicated illnesses, and the lead author of the study, Sonji Han, a professor of chemistry at North Western University, said that “the spectrum of degenerative diseases associated with the tau protein is very wide, which begins with chronic hemogenic cerebral analogy of soccer players, to the cortical cortical dougheration and Bo -core paralysis “, taking into account” creating the creation of parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts of the parts. Understanding these complex diseases. Tau -protein and so far tau diseases can only be accurately diagnosed after the death of the patient, as their brains are analyzed using cool electronic photography techniques to detect deformed fibers. To overcome the complexity of the complete “Tao” protein, the research team developed only a small part of it, called it JR2R3, with a length of at most 19 amino acids, and contains the famous P301L opener in the world of “Tao” diseases. The P301L mutation is a genetic change that occurs in the “Tao” protein, where the prolinamino acid is replaced by the place 301 with libotic amino acid. This mutation is associated with various neurological degenerative diseases, such as Alzheimer’s disease and the luxury core paralysis, as it makes the “Tao” protein more vulnerable to wrong fold and collection in pathological fibers, which accelerates the process of neurons and the decline of brain function. This mini -part designed by scientists has shown the ability to form pathological fibers and work as a ‘seed’ to stimulate the distortion of the healthy tu proteins. Han says that the team has managed to make a miniature version “do everything the complete protein does, as it leads to stimulation, congestion and even to reform other proteins.” Cooling electronic photography confirmed that the P301 millic mutation contributes to a specific type of wrong fold, often observed in the brain of patients, which is an indication of the role of the important surge in the change of the structural behavior of protein. The study expanded to reveal an incredible side so that the protein is not alone to change, but rather the water that surrounds it also changes. “The water can look randomly fluid and random, but it is in fact more organized than we think! The change in the water structure helps stabilize the fibers just as the glue supports the cutting of wood together,” says Han. These results indicate that organized water is preparing the protein councils, which can accumulate and participate in a series of continuous wrong folds. The research team aims to deepen their studies of these synthetic proteins similar to the Bryate and to investigate their abilities in the development of new diagnostic and treatment tools to combat “tau” diseases.