Protein fibrils are protein aggregates, which can be generated from food-grade proteins by unfolding and hydrolysis and can be used in a broad context of applications. At length scales above the well-established atomistic fingerprint of amyloid fibrils, these colloidal aggregates exhibit mesoscopic properties comparable to those of natural polyelectrolytes, yet with persistence lengths several orders of magnitude beyond the Debye length. This intrinsic rigidity, together with their chiral, polar and charged nature, provides these systems with a unique physical behavior.
Please join Dr. Raffaele Mezzenga as he discusses 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, illustrating how this information may 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 Dr. Mezzenga will give a few examples on how these systems can ideally suit the design of biosensors and biomaterials, cellular scaffolds, biomoimetic bones, catalytic and water purification membranes, as well as how protein fibrils allow original applications in food science and nutrition, by providing unchallenged delivery systems for nanostructured bioavailable iron.