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PEG-mimetic peptoid reduces protein fouling of polysulfone hollow fibers
[Display omitted] •Polysulfone hollow fiber membranes are modified with a peptoid (NMEG5) using polydopamine.•The addition of peptoid to the fibers increases the hydrophilicity of the fibers by 74%.•Peptoid-modified fibers have significantly decreased protein fouling with bovine serum albumin, lysoz...
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Published in: | Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2017-01, Vol.149, p.23-29 |
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Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | [Display omitted]
•Polysulfone hollow fiber membranes are modified with a peptoid (NMEG5) using polydopamine.•The addition of peptoid to the fibers increases the hydrophilicity of the fibers by 74%.•Peptoid-modified fibers have significantly decreased protein fouling with bovine serum albumin, lysozyme, and fibrinogen.•Peptoid-modified fibers show the lowest amount of fibrinogen adsorption compared to other published low fouling membranes.
Biofouling is a persistent problem for membranes exposed to blood or other complex biological fluids, affecting surface structure and hindering performance. In this study, a peptoid with 2-methoxyethyl (NMEG5) side chains was immobilized on polysulfone hollow fiber membranes to prevent protein fouling. The successful attachment of NMEG5 to the polysulfone surface was confirmed by X-ray photoelectron spectroscopy and an increase in hydrophilicity was confirmed by contact angle analysis. The NMEG5-modified surface was found to resist fouling with bovine serum albumin, lysozyme, and adsorbed significantly less fibrinogen as compared with other published low-fouling surfaces. Due to the low fouling nature and increased biocompatibility of the NMEG5 coated membranes, they have potential applicability in numerous biomedical applications including artificial lungs and hemodialysis. |
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ISSN: | 0927-7765 1873-4367 |
DOI: | 10.1016/j.colsurfb.2016.09.038 |