has many complex proteins and so have a robust system for heat-shock protein assisted folding

The researchers also pinpointed a sequence of amino acids that appears to help the Tau protein bend in different directions, which they believe could make a good target for drugs that would interfere with the formation of Tau tangles. In the Alzheimer’s affected brain, abnormal collections of the tau protein accumulate and form tangles (seen in blue) within neurons, harming synaptic communication between nerve cells. They also showed that these fibrils are more likely to form when the ends of the Tau protein are lopped off. In the new study, the researchers discovered that one segment of the Tau protein is more flexible than expected, and this flexibility helps the fibrils take on a variety of different shapes. In a new study, MIT chemists have gained insight into how these fibrils form, and identified a potential target for drugs that could interfere with this formation. Many neurodegenerative diseases, including Alzheimer’s, are characterized by tangled proteins called Tau fibrils. They’ve identified a sequence of amino acids that could be targeted by drugs to prevent the formation of these filaments.Ī new study shows that truncated versions of the Tau protein are more likely to form the sticky filaments seen in the brains of people with Alzheimer’s disease. MIT researchers have found that the Tau protein, linked to neurodegenerative diseases, forms harmful filaments more easily when its ends are cut off, and that its flexibility contributes to the varied shapes of these filaments.

Has many complex proteins and so have a robust system for heat-shock protein assisted folding