(575c) The Specific Recognition of A Collagen Mimetic Cell-Binding Peptide Sequence Derived from Type I Collagen for Different Cell Types

In recent development of biomaterials, numerous cell binding sequences have been used to convey biofunctionality to these materials. However, little has been done to study the specific recognition of different cell types to a specific collagen or ECM protein sequence. In this study, we focused on studying the affinity of different cell types for a specific cell binding sequence (GFOGER) derived from type I collagen using peptide template(PT)-assembled collagen peptides of different triple helicity as a model for natural collagen. A series of biophysical studies, including melting curve analysis and CD spectroscopy, demonstrated the presence of stable triple-helical conformation in the PT-assembled (GPO)3-GFOGER-(GPO)3, (GPO)-GFOGER-(GPO), and (Pro-Hyp-Gly)5 solution. Conversely, non-templated peptides, except (GPO)3-GFOGER-(GPO)3, showed no evidence of assembly of triple-helical structure. Biological assays, including cell adhesion, competitive inhibition, and immunofluorescence stainings, revealed a correlation of triple-helical conformation with cellular recognition of collagen mimetics in an integrin-specific way. Hep3B and L929 cells displayed significant differences in the recognition of this GFOGER sequence on the collagen mimics, mainly due to the differences in their expression of specific integrin receptors for collagen. PT-assembled (GPO)3-GFOGER-(GPO)3 was shown to perform comparably to collagen for L929, but not Hep3B, cell adhesion, suggesting the need to use specific adhesive peptide sequences to precisely controlling the adhesion for a specific type of cell.