Material surfaces that can mediate cellular interactions by the coupling of specific cell membrane receptors may allow for the design of a
biomaterial that can control cell attachment, differentiation, and tissue organization. Cell adhesion
proteins have been shown to contain minimum
oligopeptide sequences that are recognized by
cell surface receptors and can be covalently immobilized on material surfaces. In this study, cell attachment to
fluorinated ethylene propylene (
FEP) films functionalized with the
laminin-derived
oligopeptides,
YIGSR and a 19-mer
IKVAV-containing sequence, was assessed using NG108-15
neuroblastoma and PC12 cells. A radiofrequency glow discharge (RFGD) process that replaces the
FEP surface
fluorine atoms with reactive
hydroxyl functionalities was used to activate the film surfaces. The
oligopeptides were then covalently coupled to the surface by their C-terminus using a standard nucleophilic substitution reaction. The covalent attachment of the
oligopeptides to the
FEP surface was verified using electron spectroscopy for chemical analysis (ESCA). Receptor-mediated NG108-15 cell attachment on the
YIGSR-modified films was determined using competitive binding assays. Average cell attachment on the
oligopeptide immobilized films in medium containing soluble
CDPGYIGSR was reduced by approximately
a factor of 2, compared to cell attachment in serum-free medium alone. No significant decrease in cell attachment was noted in medium containing the mock
oligopeptide sequence CDPGYIGSK.
FEP films immobilized with the 19-mer
IKVAV sequence demonstrated a higher percentage of receptor mediated cell attachment on the film surfaces.(ABSTRACT TRUNCATED AT 250 WORDS)