Protein-resistant polyurethane via surface-initiated atom transfer radical polymerization of oligo(ethylene glycol) methacrylate

✍ Scribed by Zhilin Jin; Wei Feng; Shiping Zhu; Heather Sheardown; John L. Brash

• Publisher: John Wiley and Sons
• Year: 2009
• Tongue: English
• Weight: 359 KB
• Volume: 91A
• Category: Article
• ISSN: 1549-3296
• DOI: 10.1002/jbm.a.32319

✦ Synopsis

Abstract

Protein‐resistant polyurethane (PU) surfaces were prepared by surface‐initiated simultaneous normal and reverse atom transfer radical polymerization (s‐ATRP) of poly(oligo(ethylene glycol) methacrylate) (poly (OEGMA)). Oxygen plasma treatment was employed for initial activation of the PU surface. The grafted polymer chain length was adjusted by varying the molar ratio of monomer to sacrificial initiator in solution from 5:1 to 200:1. The modified PU surfaces were characterized by water contact angle, X‐ray photoelectron spectroscopy (XPS), and atomic force microscopy (AFM). Protein adsorption experiments from tris‐buffered saline (TBS) and plasma were carried out to evaluate the protein‐resistance of the surfaces. Adsorption from single and binary protein solutions as well as from plasma was significantly reduced after modification. Adsorption decreased with increasing poly(OEGMA) chain length. Fibrinogen (Fg) adsorption on the 200:1 monomer/initiator surface was in the range of 3–33 ng/cm^2^ representing 96–99% reduction compared with the unmodified PU. Fg adsorption from 0.01–10% plasma was as low as 1–5 ng/cm^2^. Moreover, binary protein adsorption experiments using Fg and lysozyme (Lys) showed that protein size is a factor in the protein resistance of these surfaces. © 2009 Wiley Periodicals, Inc. J Biomed Mater Res, 2009