Research News

Protein Chemistry: Misfolding the Way to Disease

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Science  15 Mar 1996:
Vol. 271, Issue 5255, pp. 1493-1495
DOI: 10.1126/science.271.5255.1493


Protein chemists have long been plagued by the tendency of proteins to aggregate in the test tube. But these aggregates, once considered to be worthless junk at best, are beginning to take on new meaning. Researchers are coming to realize that the test tube protein clumping is remarkably similar to the formation of the so-called “amyloid” protein deposits that are the pathological hallmarks of a dozen different diseases, including the common memory disorder Alzheimer's. Both apparently occur when normal protein folding goes awry, allowing incompletely folded protein molecules to grab onto each other and self-assemble into insoluble fibril aggregates. Work on this “junk” is not only leading to a better understanding of the amyloid diseases but also suggests some potential therapeutic strategies to combat them.