Disease-causing tangle could spawn new materials

Disease-causing tangle could spawn new materials

3:08 PM, 2nd August 2011
Disease-causing tangle could spawn new materials
A close-up view of an amyloid plaque model, showing the entangled structure of amyloid fibrils that form a sticky plaque.

 

CAMBRIDGE, US: Beside playing a role in a number of diseases, amyloids also play an important structural role in many organisms from bacteria to mammals and might point the way to a whole new category of biologically inspired synthetic materials.

Each protein normally folds itself into a specific shape that governs many aspects of its interactions with other materials and organisms. But almost all proteins and peptides (organic molecules that are similar to proteins but shorter) can alternatively form amyloids, which form dense, concentrated masses instead of precisely folded shapes.

Now Markus Buehler, an associate professor of civil and environmental engineering at MIT, and Tuomas Knowles, a lecturer in physical chemistry at the University of Cambridge in the UK, have reviewed and analyzed the details of how amyloids form and their potential as the basis for new materials. Their analysis, encompassing both experimental and computational approaches, was published July 31 in the journal Nature Nanotechnology. The work was funded primarily by the Office of Naval Research with additional support from the National Science Foundation, the Army Research Office and the Air Force Office of Scientific Research.

Normal proteins naturally break down and their constituent parts are recycled within a cell, but amyloids stubbornly resist that breakdown - one of the features that give them their unusual strength as structural materials.

“They are even sticky in the brain, which is why they don’t break down easily. They interfere with the functioning of tissues,” said Buehler.  

Concentrations of amyloids within the human brain may play a role in the onset of Alzheimer’s disease, Parkinson’s disease and other neurological conditions.

In addition to their stickiness, amyloids are exceptionally strong and resilient structures that can be used to form internal scaffolding to support the structure of cells. Buehler and Knowles found that amyloids show exceptional stiffness even within tissues, which may contribute to their role in promoting disease.

A first step toward the exploitation of amyloids in engineering, Buehler said, would be to produce protein materials with specific desired attributes, such as structures that attach themselves to atoms of metal.  

Buehler said amyloids might be used to produce nanowires for use in highly miniaturized circuits, and it’s even possible to produce more complex structures such as coaxial nanowires.

Other applications under development include the use of amyloid fibrils as templates to control the orientation of polymers in new organic solar cells, their use for controlled-release drug delivery, and for producing three-dimensional scaffolding for tissue repair in the brain - a remarkable turnabout of their destructive role in neurodegenerative disease.

(C) Massachusetts Institute of Technology News

 

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