Functional peptides are attractive as novel therapeutic reagents because their amino acid sequences are flexible in adopting and mimicking the local functional features of proteins. These peptides are of low molecular weight, synthetically versatile and inexpensive to produce, suggesting that they can be used as drug targeting, potent, stable and bioavailable agents. A short bioactive peptide is expected to be more beneficial in regenerative medicine than an entire protein because of the lower antigenicity of short amino acid sequences. We detected core peptides from human laminin that are involved in adhesion and spreading, which are the first steps of various cells including osteogenic cells, in becoming functional. In this experiment, we detected adhesion and spreading of osteoblast-like cells seeded on the core peptide-coated surface. These in vitro data are related to the research article, entitled "Identification of a bioactive core sequence from human laminin and its applicability to tissue engineering" (Yeo et al., 2015) [1].