The specific recognition of a collagen mimetic cell-binding peptide sequence derived from type I collagen for different cell types

Abstract

In this study, the affinity of two different cell types towards a specific cell binding sequence (GFOGER) derived from type I collagen using peptide template (PT)-assembled collagen peptides as a model for natural collagen was examined. 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. Biological assays, including cell adhesion, competitive inhibition, and immunofluorescence staining, revealed a correlation of triple-helical conformation with the cellular recognition of GFOGER in an integrin-specific manner. Hep3B and L929 cells displayed significant differences in the recognition of GFOGER. The result showed that one specific cell binding motif may not be sufficient to mimic the ECM microenvironment.