Screening of Cell-Adhesive Peptide from the Human Laminin-5 α3 Chain Globular 2 and 3 Domains
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 <I>α</I>3 chain globular (LG) 2 and 3 domains interact with integrin <I>α</I>3<I>β</I>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 (LN<SUB>1143–1148</SUB>) and GLRLLI (LN<SUB>1239–1244</SUB>) peptides showed about 2.5-fold increase compared to no peptide. From the adhesion inhibition assay, NFEGCI (LN<SUB>1271–1276</SUB>) and NQLLQD (LN<SUB>1333–1338</SUB>) peptides were seen to interact with integrin <I>α</I>3<I>β</I>1.
- Journal of chemical engineering of Japan
Journal of chemical engineering of Japan 41(3), 206-209, 2008-03-01
The Society of Chemical Engineers, Japan