University of Cambridge > Talks.cam > Biophysical Seminar Series 2016/17 > The Evolution of Amyloid Fibrils from Pathological to Functional Materials

The Evolution of Amyloid Fibrils from Pathological to Functional Materials

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If you have a question about this talk, please contact Francesco Simone Ruggeri.

Amyloid protein fibrils were originally known for their implication in several aberrant neurodegenerative pathologies. Today we know that amyloid fibrils can be produced in-vitro from a much broader range of proteins, including non-toxic, food-grade proteins. The resulting protein fibrils possess unique chemical, structural and colloidal properties which make them of possible use in an extraordinary vast context of applications. Their stiffness combined with their chiral, polar and charged nature, provides these systems with some unique physical behavior. In this talk I will discuss our current understanding on the mesoscopic properties of amyloid fibrils at the single molecule level, the implication of their semiflexible nature on their liquid crystalline properties, and I will illustrate how this information prove useful in understanding their collective behavior in bulk and when adsorbed at liquid interfaces. By the careful exploitation of the physical properties of amyloid fibrils, the design of advanced materials with unprecedented physical properties become possible, and I will give a few examples on how these systems can ideally suit the design not only of complex food systems, but also of biosensors, biomaterials, cellular scaffolds, catalytic and water purification membranes, making them promising candidates for building blocks in advanced materials and emerging nanotechnologies.

This talk is part of the Biophysical Seminar Series 2016/17 series.

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