Our surface mediated amyloid aggregation model is a significant departure from the current model in which amyloid aggregation is linked with elevated synthesis of amyloid proteins and their accumulation in the cell to initiate the aggregation process. The lack of evidence for the change of amyloid protein level during the disease progression is a weak point of this model. Our model does not require an elevation of amyloid synthesis as the on-surface assembly can occur at the nanomolar concentration range of the protein. The approaches described in this paper can be extended to various types of surface, so future studies will provide detailed characterization of the on-surface aggregation process and pinpoint possible changes in cellular membrane defining the disease prone state of the organism.