Research into amyloids was initially motivated by pathogenic amyloids involved in disease states such as Alzheimer's; however, new research implicates small oliogmeric species and not the mature fibers. This lack of toxicity has allowed for the development of amyloid-based biomaterials for use as nanowires, biosensors, and tissue regeneration. The directed self-assembly of peptides into amyloid-like fibers for use as biomaterials requires the ability to control both the nucleation location and growth direction of the fiber. We have used Atomic Force Microscopy to repeatedly stretch Silk-Elastin-Like Peptide Polymer (SELP) in the normal direction using continuous pulling in a force acquisition mode which has the ability to create nanodots of SELP at a specified location which are capable of nucleating SELP nanofibers. This work, if generalized to other amyloidogenic systems, may aid in the mechanistic understanding of the assembly process of both pathogenic and functional amyloids.