Document Detail


Formation and antifouling properties of amphiphilic coatings on polypropylene fibers.
MedLine Citation:
PMID:  23013136     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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 (GA) in the presence of sodium borohydride (NaBH4). 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 (ATRP). 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. Anti-fouling 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 to 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 top-most layer of the amphiphilic coating and its anti-fouling capability.
Authors:
Kiran K Goli; Orlando Jose Rojas; Jan Genzer
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-9-27
Journal Detail:
Title:  Biomacromolecules     Volume:  -     ISSN:  1526-4602     ISO Abbreviation:  Biomacromolecules     Publication Date:  2012 Sep 
Date Detail:
Created Date:  2012-9-27     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100892849     Medline TA:  Biomacromolecules     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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