The grafting of active peptides onto structurally stable scaffold proteins is effective for the generation of functional proteins. In this study， we aimed to develop a grafting method using ubiquitin as a scaffold protein. Ubiquitin is a small protein consisting of 76 amino acid residues that is highly stable against heat and pH stress， which are desirable characteristics for a scaffold protein. Moreover， its structure is maintained even if it is split or additional residues are inserted. Therefore， we assumed that grafting of an active peptide into ubiquitin would result in a functional protein. As a proof of concept， we developed the ubiquitin-based binder (UbB)， into which the p53 (17-28) peptide was inserted between Ile36 and Pro37. The p53 (17-28) peptide， utilized as a model active peptide in this work， is known to bind to mouse double minute 2 homolog (Mdm2). Size exclusion chromatography and circular dichroism indicated that UbB maintained a similar structure to that of ubiquitin. The affinity for Mdm2 measured by surface plasmon resonance was 292 times greater than that of the p53 (17-28) peptide. These observations indicate that ubiquitin is a robust scaffold for peptide grafting. We hope that this study will aid further development of ubiquitin-based protein engineering.