Researchers at Emory University and Argonne National Laboratory have discovered a new method to manipulate the self-assembly and formation of amyloid fibrils, a major component of brain plaques associated with Alzheimer’s disease, thereby opening new avenues for examination of their formation and for the construction of robust nanotubes that have potential applications in research, industry and medicine.
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.
Deb Hammacher | EurekAlert!
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