Certain short amino acid chains, the building blocks of proteins, are capable of self-assembly into the disease-causing amyloid fibrils of Alzheimer's. Emory biochemistry professor David Lynn and his colleagues have now enticed these amyloid peptides to self-assemble into well-defined nanotubes 15 billionths of a meter across. Such nanotubes can now serve as minute scaffolds to build nanotechnological devices with potential applications in many fields. These findings are published in the May 21 issue of the Journal of the American Chemical Society in their paper "Exploiting Amyloid Fibril Lamination for Nanotube Self-Assembly."
"We took what we know about amyloid fibril self-assembly, and used that information to construct novel, self-assembling nanotubes. The creation of these new structures will in turn teach us more about the physical properties of amyloids and the pathways to their formation, which puts us in a better position to understand why they are so damaging and cause disease," says Lynn.
The discovery underscores the potential of the emerging field of "synthetic biology," demonstrating the use of self-assembling elements that nature goes to great lengths to avoid, and converting them to new functional materials, Lynn says.
"Nature goes to extreme measures to keep these amyloids from forming, but nature still hasn't figured out a way on its own to totally control the formation of them. What we have uncovered is a way to control and manipulate the amyloid in a way that nature can't, so that it acts differently and takes on a new
Contact: Deb Hammacher
Emory University Health Sciences Center