The aggregation of α-synuclein that contributes to Parkinson's disease has been blocked in an animal model of the condition, which is promising but needs much more testing: researchers "report the development of a novel compound known as a 'molecular tweezer,' which in a living animal model blocked α-synuclein aggregates from forming, stopped the aggregates' toxicity and, further, reversed aggregates in the brain that had already formed. And the tweezers accomplished this without interfering with normal brain function. ... finding a therapy that targets only the aggregates is a complicated process ... In Parkinson's, for example, the protein implicated in the disorder, α-synuclein, is naturally ubiquitous throughout the brain. ... Its normal function is not well understood, but it may play a role in aiding communication between neurons. The trick, then, is to prevent the α-synuclein protein aggregates and their toxicity without destroying α-synuclein's normal function, along with, of course, other healthy areas of the brain. [The researchers used] a particular molecular tweezer he had developed called CLR01. Molecular tweezers are complex molecular compounds that are capable of binding to other proteins. Shaped like the letter 'C,' these compounds wrap around chains of lysine, a basic amino acid that is a constituent of most proteins. Working first in cell cultures, the researchers found that CLR01 was able to prevent α-synuclein from forming aggregates, prevent toxicity and even break up existing aggregates. ... The researchers next tried their tweezers in a living animal, the zebrafish ... Using a transgenic zebrafish model for Parkinson's disease, the researchers added CLR01 and used fluorescent proteins to track the tweezer's effect on the aggregations. They found that, just as in cell cultures, CLR01 prevented α-synuclein aggregation and neuronal death, thus stopping the progression of the disorder in the living animal model."