The utilization of biomaterials such as proteins or peptides has recently been focused on as an attractive way to construct nanomaterials by ldquo;bottom-uprdquo; strategy. We focus on α-synuclein as a novel scaffold material for functional nanomaterial fabrication. This protein constructs an amyloid-like nanostructure by self-assembly under mild conditions. In this paper, we demonstrate nanomaterial fabrication by utilizing two peptide fragments of the non-amyloid-β component of Alzheimer's disease amyloid region, which is the key region for α-synuclein fibrillation. One of these peptide fragments contains the sequence corresponding to residues 66–82 of wild-type α-synuclein, while the other contains the same region from the Val70Thr/Val71Thr mutant, whose character is drastically different. In this paper, we confirmed that these two peptides individually formed different rod-like structures. Moreover, these peptides modify the fibril nanostructure of full-length α-synuclein, and these effects depend on the peptide sequences. Therefore, we propose the combination of amyloid-forming protein, and its partial peptide fragments with some mutations have a potential for novel nanomaterial fabrication.