Formation and antifouling properties of amphiphilic coatings on polypropylene fibers.

Kiran K Goli, Orlando J Rojas, Jan Genzer

Index: Biomacromolecules 13(11) , 3769-79, (2012)

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Abstract

We describe the formation of amphiphilic polymeric assemblies via a three-step functionalization process applied to polypropylene (PP) nonwovens and to reference hydrophobic self-assembled n-octadecyltrichlorosilane (ODTS) monolayer surfaces. In the first step, denatured proteins (lysozyme or fibrinogen) are adsorbed onto the hydrophobic PP or the ODTS surfaces, followed by cross-linking with glutaraldehyde in the presence of sodium borohydride (NaBH(4)). The hydroxyl and amine functional groups of the proteins permit the attachment of initiator molecules, from which poly (2-hydroxyethyl methacrylate) (PHEMA) polymer grafts are grown directly through "grafting from" atom transfer radical polymerization. The terminal hydroxyls of HEMA's pendent groups are modified with fluorinating moieties of different chain lengths, resulting in amphiphilic brushes. A palette of analytical tools, including ellipsometry, contact angle goniometry, Fourier transform infrared spectroscopy in the attenuated total reflection mode, and X-ray photoelectron spectroscopy is employed to determine the changes in physicochemical properties of the functionalized surfaces after each modification step. Antifouling properties of the resultant amphiphilic coatings on PP are analyzed by following the adsorption of fluorescein isothiocyanate-labeled bovine serum albumin as a model fouling protein. Our results suggest that amphiphilic coatings suppress significantly adsorption of proteins as compared with PP fibers or PP surfaces coated with PHEMA brushes. The type of fluorinated chain grafted to PHEMA allows modulation of the surface composition of the topmost layer of the amphiphilic coating and its antifouling capability.