The arginine-glycine-aspartic acid (RGD) motif is a cell adhesion sequence that binds to integrins. Some RGD-containing peptides promote adhesion of both embryonic stem cells and induced pluripotent stem cells (iPSCs), but not all such RGD-containing peptides are active. In this study, we elucidated the role of RGD-neighboring sequences on iPSC adhesion using diverse synthetic peptides. Various RGD-containing peptides with different RGD-neighboring sequences were immobilized on maleimide-functionalized bovine serum albumin (Mal-BSA)-coated plates via a thiol-maleimide reaction, and cell adhesion activity was evaluated using several types of cells, including iPSCs. As a result, only two RGD-containing peptides, vnRGD and bspRGD, promoted iPSC adhesion. We revealed that RGDVF and RGDNY are the minimal sequences of the two peptides. We also found that the trimeric RGD motif binds to integrin αvβ3, but not to integrin αvβ5, whereas RGDVF and RGDNY sequences bind to both integrins αvβ3 and αvβ5. This study revealed that iPSC adhesion requires RGDX1X2 sequences, where X1X2 residues are VF and NY, respectively, and that the X1X2 residues are essential for iPSC adhesion because iPSCs express integrin αvβ5 but do not express αvβ3. These findings will provide important new insights into the interaction between the RGD motifs and integrins.