In this work, we investigated the ability of amyloid fibrils derived from two food proteins to heterologously seed the aggregation of the PD-related aSyn protein. While β-lactoglobulin amyloid fibril seeds were not able to induce aSyn aggregation, we identified a fibril surface–mediated nucleation mechanism for the seeding of aSyn aggregation by hen egg white lysozyme fibrils. We could attribute this difference in seeding capacity to differences in the affinity of aSyn for both fibril surfaces and aSyn region responsible for this surface binding. CLICK TO REVIEW