Peptoid-containing collagen mimetics with cell binding activity

Collagen mimetic peptides containing the peptoid residue Nleu (Goodman Bhum ralkar, Jefferson, Kwak, Locardi. Biopolymers 1998;47:127-142) were tested for interactions with epithelial cells and fibroblasts. Molecules containin g the sequence Gly-Pro-Nleu with a minimum of nine repeats showed cell bind ing activity. The activity of these molecules appeared to be conformational ly sensitive, with the triple-helical form being preferred. When immobilize d on a surface, the (Gly-Pro-Nleu)(10)-Gly-Pro-NH2 sequence stimulated the attachment and growth of corneal epithelial cells and fibroblasts and the m igration of epithelial tissue. The peptide sequence KDGEA inhibited cell at tachment to the (Gly-Pro-Nleu)(10)-Gly-Pro-NH2 sequence, suggesting that ce ll binding to this collagen mimetic involves the alpha 2 beta 1 heterodimer integrin receptor. Interestingly, peptides containing the sequence (GlyNle u-Pro-)(10)-NH2 did not have cell binding activity. The discovery that trip le-helical peptides containing the Gly-Pro-Nleu sequences interact with cel ls opens up new opportunities in the design of collagen mimetic biomaterial s. (C) 2000 John Wiley & Sons, Inc.