EventProf. Raffaele Mezzenga

Nanotechnology and Materials Science using Protein Nanofibrils

  1. Understanding amyloid aggregation by statistical analysis of atomic force microscopy images” Adamcik et al., Nature nanotechnology, 5, 423 (2010).
  2. Biodegradable Nanocomposites of Amyloid Fibrils and Graphene with Shape Memory and Enzyme Sensing Properties” Li et al. Nature nanotechnology, 7, 421 (2012).
  3. Amyloid–carbon hybrid membranes for universal water purification” Bolisetty et al. Nature nanotechnology, 11, 365 (2016).
  4. Amyloid fibril systems reduce, stabilize and deliver bioavailable nanosized iron” Shen et al. Nature nanotechnology, 12, 642 (2017).

Protein fibrils are protein aggregates, which can be generated from food-grade proteins by unfolding and hydrolysis. Differently from the pathological homologue amyloid fibrils, which form in vivo from toxic protein and peptides, the resulting protein fibrils formed from food protein precursors 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 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 of biosensors and biomaterials, cellular scaffolds, biomoimetic bones, catalytic and water purification membranes. In the end of the talk I will emphasize how the non-toxic nature of the protein fibrils considered allow original applications in food science and nutrition, by providing unchallenged delivery systems for nanostructured bioavailable iron.

About The Speaker


Raffaele Mezzenga received his master degree (Summa Cum Laude) from Perugia University, Italy, in Materials Science and Engineering, while actively working for the European Center for Nuclear Research (CERN) and NASA on elementary particle-polymer interactions (NASA Space Shuttle Discovery mission STS91). In 2001 he obtained a PhD in Polymer Physics from EPFL Lausanne, focusing on the thermodynamics of reactive polymer blends. He then spent 2001-2002 as a postdoctoral scientist at University of California, Santa Barbara, working on the self-assembly of polymer colloids. In 2003 he moved to the Nestlé Research Center in Lausanne as research scientist, working on the self-assembly of surfactants, natural amphiphiles and lyotropic liquid crystals. In 2005 he was hired as Associate Professor in the Physics Department of the University of Fribourg, and he then joined ETH Zurich on 2009 as Full Professor. In 2016 he founded BluAct Technologies, an ETH Spinoff exploiting a revolutionary technology for water purification, where he currently serves as Chief Scientific Officer. His research focuses on the fundamental understanding of self-assembly processes in polymers, lyotropic liquid crystals, food and biological colloidal systems. Prof. Mezzenga has been a visiting Professor from Helsinki University of Technology (now Aalto University), a Nestlé Distinguished Scientist, and recipient of several international distinctions such as the 2011 John H. Dillon Medal and the 2017 Fellowship of the American Physical Society [citation: “For exceptional contributions to the understanding of self-assembly principles and their use to design and control materials with targeted functionalities“], the 2011 AOCS Young Scientist Research Award [citation: “For his pioneering work on polymers, colloids and liquid crystals“], and the 2013 the Biomacromolecules/Macromolecules 2013 Young Investigator Award of the American Chemical Society [citation: “In recognition of his outstanding contributions to the fundamental understanding of self-assembly processes in polymers and biological colloidal systems”]