Journal of Chemical Engineering of Japan, Vol.41, No.3, 206-209, 2008
Screening of cell-adhesive peptide from the human laminin-5 alpha 3 chain globular 2 and 3 domains (SC)
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 alpha 3 chain globular (LG) 2 and 3 domains interact with integrin alpha 3 beta 1 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 alpha 3 beta 1.