Editor's Choice Main Category: Parkinson's Disease Article Date: 02 May 2012 - 11:00 PDT

email to a friend printer friendly opinions

Current Article Ratings:

4.5 (2 votes)

By using powerful computer tools and laboratory tests, the scientists managed to obtain a step-by-step explanation of how a "protein-run-amok" aggregates within the membranes of neurons, puncturing them and causing Parkinson's disease symptoms. The process describes how -synuclein (a-syn) can turn against us, especially as we get older. The results of the model demonstrate how -syn monomers penetrate cell membranes and how they become coiled and aggregate within nanoseconds into dangerous ring structures that are harmful for neurons.

Lead researcher Igor Tsigelny, a research scientist at the San Diego Supercomputer Center and Department of Neurosciences at UC San Diego, declared:

Numerous cases of familial Parkinson's disease are caused by a limited number of protein mutations, the most toxic of which is A53T. Tsigelny's team demonstrated that the mutant form of -syn both penetrates neuronal membranes substantially faster compared with a normal -syn, and that the mutant protein also accelerates ring formation.

Tsigelny explained:

The researchers discovered that their modeling results also proved consistent with electron microscopic images of neurons in Parkinson's disease patients that have shown damaged neurons are riddled with ring structures.

The researchers immediately turned to search for drug candidates that can inhibit ring formation in neuron membranes. The highly complex modeling consists of various sophisticated scientific realms, which intersect between chemistry, physics, and statistical probabilities. A wide spectrum of interacting forces within this realm cause circumstances comparable to an earthquake, in which the a-syn proteins bump and tremble, coil and uncoil and join up in pairs or larger groups.

The rest is here:
Once-Marginalized Parkinson's Disease Theory May Be Valid