Structure and mechanics of amyloid fibers

Many proteins of diverse sequence, structure and function have the ability to form amyloid fibrils  when partially unfolded. These highly ordered nanofibrils exhibit  remarkable mechanical properties. Since the formation is a simple self-assembly process and amyloids are biocompatible and robust under extreme conditions, they are attractive candidates for applications in materials science, tissue engineering and food science. Amyloid fibers have also been linked to conformational diseases such as Alzheimer’s Disease, where aggregation of amyloid fibers were found in tissue.  Polyphenols are a possible candidate to control amyloid formation and stability, as it was found that these flavonoids interact specifically with amyloids. In order  to understand and control the relation between the structure of amyloid fibrils on the supramolecular scale and the ultimate structure and mechanics of the self-assembled networks on the macroscopic scale, the self-assembly of the model proteins  Alzheimer amyloid β(1-42) and the milk protein β-lactoglobulin, which is abundant  in whey, are studied using a combination of microscopy, (micro) rheology and atomic force microscopy. The resulting fundamental insights are essential for the development of new therapeutics to treat fibrillisation-related afflictions, the rational design of novel edible and biodegradable biomaterials and for optimizing industrial food processing.

More information: Corianne Gelderloos and Jeanette Nguyen

Collaborators: Mischa Bonn (AMOLF) and Krassimir Velikov (Unilever)