The fibril zipper - The Scientist - Magazine of the Life Sciences
Abstract
The paper: R. Nelson et al., "Structure of the cross-β spine of amyloid-like fibrils," Nature, 435:773-8, 2005. (Cited in 119 papers) | [PubMed] The finding: In 2005, Howard Hughes Medical Institute Investigator David Eisenberg and his team at the University of California Los Angeles successfully determined the atomic structure of the protein fibrils formed from sub-pieces of the yeast protein Sup35. The jargon: The team was able to image the protein fibril structures from pieces of the protein only seven and then six amino acids in length, each showing their long side chains bound together like Velcro. Eisenberg's team termed this effect the "Dry Steric Zipper," referring to the fact that the structure forms by dehydrating the region between the protein sheets to form an interlocking zone. The follow up: In subsequent research, using the original six-amino-acid structure as a template, they have been able to find human sequences likely to form amyloid-like fibrils in proteins like insulin and β2-microglobulin. The future: Eisenberg has been collaborating with researchers at the University of Washington to predict which portions of proteins are responsible for forming amyloids, hopefully to move beyond structure and into function. "By seeing the structures it may