The role of surfaces on amyloid formation

Interfaces can strongly accelerate or inhibit protein aggregation, destabilizing proteins that are stable in solution or, conversely, stabilizing aggregation-prone. Although this behaviour is well-known, our understanding of the molecular mechanisms underlying surface-induced aggregation still largely incomplete. A major challenge represented by high number physico-chemical parameters involved, which highly specific to considered combination protein, surface properties, and conditions. The key aspect determining role interfaces relative propensity aggregate at with respect bulk. In review, we discuss multiple determinants regulate balance. We summarize current experimental techniques aimed characterizing interfaces, highlight need complement analysis theoretical modelling. particular, illustrate how chemical kinetic be combined methods provide insights into under both stagnant agitation recent progress study important amyloids systems, focusing on selected relevant interfaces.