Abstract
Laminin (LN)-5 is an epithelial specific adhesion component and a main ligand for keratinocyte. It regulates various cellular functions, including cell adhesion, spreading, and motility. The human LN-5 α3 chain globular (LG) 2 and 3 domains interact with integrin α3β1 selectively. Using peptide array-based interaction assay, screening of cell-adhesive peptide was performed with 6-mer peptide library of LG-2 and -3 domains. Eight peptides with high cell-adhesive effects were found, and the activity of DWKLVR (LN1143–1148) and GLRLLI (LN1239–1244) peptides showed about 2.5-fold increase compared to no peptide. From the adhesion inhibition assay, NFEGCI (LN1271–1276) and NQLLQD (LN1333–1338) peptides were seen to interact with integrin α3β1.
