Misfolded globular amyloid proteins embedded in cell membranes may create ion channel-like structures, disrupting the cell’s electrical properties and leading to degeneration, according to research scientist Ratnesh Lal of UCSB’s Neuroscience Research Institute.

Using atomic force microscopy and a battery of other diagnostic devices, Lal and his team examined the 3D structure of misfolded amyloid proteins associated with Alzheimer’s, Parkinson’s, and other neurodegenerative diseases. All were found to form artificial channels, or pores, through cell membranes.

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After analyzing more than 58,000 compounds, three small molecules have been discovered that appear to inhibit a key step in the growth of fibrous tangles of the tau protein that characterize the brains of Alzheimer’s victims, reports Ken Kosik, co-director of the Neuroscience Research Institute.

Various enzymes pick up a phosphate molecule and attach it to a tau protein, turning the protein dysfunctional through a process called phosphorylation. The place where these enzymes connect to the phosphate usually has a pocket. The three molecules identified bind in or near the pocket, at least partially inhibiting the phosphorylation, explained Kosik.

He emphasized that Alzheimer’s involves a complicated series of genetic steps and no one gene or protein causes all the damage. However, this research opens doors to new drugs that, perhaps working in combination, could add up to a treatment of the disease.

More information: <www.ia.ucsb.edu/pa/archive.aspx>.