Peptoid-containing collagen mimetics with cell binding activity.

Abstract

Collagen mimetic peptides containing the peptoid residue Nleu (Goodman Bhumralkar, Jefferson, Kwak, Locardi. Biopolymers 1998;47:127-142) were tested for interactions with epithelial cells and fibroblasts. Molecules containing the sequence Gly-Pro-Nleu with a minimum of nine repeats showed cell binding activity. The activity of these molecules appeared to be conformationally sensitive, with the triple-helical form being preferred. When immobilized on a surface, the (Gly-Pro-Nleu)(10)-Gly-Pro-NH(2) sequence stimulated the attachment and growth of corneal epithelial cells and fibroblasts and the migration of epithelial tissue. The peptide sequence KDGEA inhibited cell attachment to the (Gly-Pro-Nleu)(10)-Gly-Pro-NH(2) sequence, suggesting that cell binding to this collagen mimetic involves the alpha2beta1 heterodimer integrin receptor. Interestingly, peptides containing the sequence (GlyNleu-Pro-)(10)-NH(2) did not have cell binding activity. The discovery that triple-helical peptides containing the Gly-Pro-Nleu sequences interact with cells opens up new opportunities in the design of collagen mimetic biomaterials.

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@article{Johnson2000PeptoidcontainingCM, title={Peptoid-containing collagen mimetics with cell binding activity.}, author={Gabriel S Johnson and Michael Jenkins and Keith Mclean and H J Hans J Griesser and Jinhak Kwak and Max Lawrence Goodman and John G. Steele}, journal={Journal of biomedical materials research}, year={2000}, volume={51 4}, pages={612-24} }