Cell adhesive PET membranes by surface grafting of RGD peptidomimetics.
A non-peptide mimic of the Arg-Gly Asp (RGD) active sequence of adhesive proteins (such as vitronectin) has been equipped with two different spacer-arms for surface anchorage. The covalent grafting on poly(ethylene terephthalate) (PET) membrane was realized via the activation of the hydroxyl polymer chain-ends by tosylation followed by nucleophilic substitution. The surface density of peptidomimetics was determined by X-ray photoelectron spectroscopy (XPS), on the basis of F/C atomic ratios since a fluorine tag was incorporated into the RGD-like compounds. The biological activity of soluble peptidomimetics was evaluated versus isolated human integrin alpha(v)beta(3) (vitronectin receptor), and versus CaCo2 cells. Inhibition of cellular adhesion was observed after pre-incubation of CaCo2 cells with soluble peptidomimetics. On the other hand a significant promotion of cellular adhesion resulted from the surface grafting of peptidomimetics on the PET culture substrate. The best performance was obtained with the RGD-like integrin ligand bearing a triethylene glycol spacer-arm.
Biltresse
Stéphane
S
Unité de chimie Organique et Médicinale, Université catholique de Louvain, Bâtiment Lavoisier, Place Louis Pasteur 1, B-1348 Louvain-la-Neuve, Belgium.
Attolini
Mireille
M
Marchand-Brynaert
Jacqueline
J
D002448:Cell Adhesion; D002460:Cell Line; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008567:Membranes, Artificial; D018716:Molecular Mimicry; D009842:Oligopeptides / Q000737:chemistry*; D013499:Surface Properties
D008567:Membranes, Artificial; D009842:Oligopeptides; C047981:arginyl-glycyl-aspartic acid