Amyloid, cause of Alzheimer's disease, could be a useful optical nanomaterial or even metamaterial

Göteborg, Sweden--Researchers from Chalmers University of Technology have discovered that amyloid, the misfolded protein that is a cause of Alzheimer’s, Parkinson’s, and Creutzfeldt-Jakob disease, also reacts to multiphoton radiation in a way that the healthy (non-misfolded) protein does not.¹ Thus, amyloid could become a building block for future nanomaterials.

“It is possible to create these protein aggregates artificially in a laboratory,” says Piotr Hanczyc, one of the researchers who made the discovery. “By combining them with other molecules, one could create materials with unique characteristics.” The researchers found that amyloid exhibits two-photon, three-photon, or even higher multiphoton absorption, with the dominance of a particular process depending on the wavelength of light used.

Amyloid aggregates are as hard and rigid as steel. The difference is that steel is much heavier and has defined material properties, whereas amyloids can be tuned for specific purposes. By attaching a material’s molecules to the dense amyloid, its characteristics change. “This was already known, but what has not been known is that the amyloids react to multiphoton irradiation,” says Piotr Hanczyc. “This opens up new possibilities to also change the nature of the material attached to the amyloids.”

The amyloids are shaped like discs, densely piled upon each other. When a material is merged with these discs, its molecules end up so densely and regularly placed that they can communicate and exchange information -- thus the potential to change the material’s characteristics.

Piotr Hanczyc, one of the researchers who made the discovery, believes that someday scientists may use the material properties of amyloid fibrils in research on optical metamaterials.

REFERENCE:

1. Piotr Hanczyc et al., Nature Photonics (2013); doi: 10.1038/nphoton.2013.282