Advertisement

If you have an ACS member number, please enter it here so we can link this account to your membership. (optional)

ACS values your privacy. By submitting your information, you are gaining access to C&EN and subscribing to our weekly newsletter. We use the information you provide to make your reading experience better, and we will never sell your data to third party members.

ENJOY UNLIMITED ACCES TO C&EN

Physical Chemistry

Steric Zippers Play Key Role In Amyloid Fibrils

Study indicates that Alzheimer's, type 2 diabetes, and other degenerative diseases are closely related at the molecular level

by Stu Borman
May 3, 2007

IN COMMON
[+]Enlarge
Credit: Michael Sawaya and David Eisenberg/UCLA
Microcrystals of amyloid structures studied by Eisenberg and coworkers (four shown) share a steric zipper motif.
Credit: Michael Sawaya and David Eisenberg/UCLA
Microcrystals of amyloid structures studied by Eisenberg and coworkers (four shown) share a steric zipper motif.

Two years ago, David Eisenberg of the University of California, Los Angeles, and a collaborative international group obtained the first atomic structure of an amyloid fibril formed from a yeast prion protein and found that an interdigitated β-sheet structure called a steric zipper was essential to fibril formation (C&EN, June 13, 2005, page 9).

Now, the same group has confirmed that steric zippers are a common structural feature in such aggregates by determining the atomic structures of microcrystals formed by 30 peptides associated with Alzheimer's disease, Parkinson's disease, type 2 diabetes, Creutzfeldt-Jakob disease, and other amyloid-related conditions (Nature, DOI: 10.1038/nature05695).

The researchers used specialized techniques, including synchrotron radiation microcrystallography, to obtain structures of the amyloid microcrystals, which otherwise would be too small to permit structural analysis. The work suggests that "amyloid diseases are similar not only on the fibril level, but also on the molecular level," the researchers write.

Article:

This article has been sent to the following recipient:

0 /1 FREE ARTICLES LEFT THIS MONTH Remaining
Chemistry matters. Join us to get the news you need.