Protein resistant surfaces: Comparison of acrylate graft polymers bearing oligo-ethylene oxide and phosphorylcholine side chains
Biointerphases volume 1, pages 50–60 (2006)
The objective of this work was to compare poly(ethylene glycol) (PEG) and phosphorylcholine (PC) moieties as surface modifiers with respect to their ability to inhibit protein adsorption. Surfaces were prepared by graft polymerization of the methacrylate monomers oligo(ethylene glycol) methyl ether methacrylate (OEGMA, MW 300, PEG side chains of length n=4.5) and 2-methacryloyloxyethyl phosphorylcholine (MPC, MW295). The grafted polymers thus contained short PEG chains and PC, respectively, as side groups. Grafting on silicon was carried out using surface-initiated atom transfer radical polymerization (ATRP). Graft density was controlled via the surface density of the ATRP initiator, and chain length of the grafts was controlled via the ratio of monomer to sacrificial initiator. The grafted surfaces were characterized by water contact angle, x-ray photoelectron spectroscopy, and atomic force microscopy. The effect of graft density and chain length on fibrinogen adsorption from buffer was investigated using radio labeling methods. Adsorption to both MPC- and OEGMA-grafted surfaces was found to decrease with increasing graft density and chain length. Adsorption on the MPC and OEGMA surfaces for a given chain length and density was essentially the same. Very low adsorption levels of the order of 7 ng/cm2 were seen on the most resistant surfaces. The effect of protein size on resistance to adsorption was studied using binary solutions of lysozyme (MW 14 600) and fibrinogen (MW 340 000). Adsorption levels in these experiments were also greatly reduced on the grafted surfaces compared to the control surfaces. It was concluded that at the lowest graft density, both proteins had unrestricted access to the substrate, and the relative affinities of the proteins for the substrate (higher affinity of fibrinogen) determined the composition of the layer. At the highest graft density also, where the adsorption of both proteins was very low, no preference for one or the other protein was evident, suggesting that adsorption did not involve penetration of the grafts and was occurring at the outer surface of the graft layer. It thus seems likely that preference among different proteins based on ability to penetrate the graft layer would occur, if at all, at a grafting density intermediate between 0.1 and 0.39 /cm2. Again the MPC and OEGMA surfaces behaved similarly. It is suggested that the main determinant of the protein resistance of these surfaces is the “water barrier layer” resulting from their hydrophilic character. In turn the efficacy of the water barrier depends on the monomer density in the graft layer.
Proteins at Interfaces II, Fundamentals and Applications, edited by T. A. Horbett and J. L. Brash, ACS Symposium Series No. 602 (American Chemical Society, Washington, DC, 1995).
D. G. Castner and B. D. Ratner, Surf. Sci. 500, 28 (2002).
J. L. Brash, J. Biomater. Sci., Polym. Ed. 11, 1135 (2000).
B. D. Ratner and S. J. Bryant, Annu. Rev. Biomed. Eng. 6, 41 (2004).
B. Kasemo, Surf. Sci. 500, 656 (2002).
J. H. Lee and J. D. Andrade, Prog. Polym. Sci. 20, 1043 (1995).
P. Vermette and L. Meagher, Colloids Surf., B 28, 153 (2003).
H. J. Mathieu, Y. Chevolot, L. Ruiz-Taylor, and D. Leonard, Adv. Polym. Sci. 162, 1 (2003).
Y. Iwasaki and K. Ishihara, Anal. Bioanal. Chem. 381, 534 (2005).
S. I. Jeon, J. H. Lee, J. D. Andrade, and P. G. De Gennes, J. Colloid Interface Sci. 142, 149 (1991).
I. Szleifer, Biophys. J. 72, 595 (1997).
T. McPherson, A. Kidane, I. Szleifer, and K. Park, Langmuir 14, 176 (1998).
M. Jonsson and H. O. Johansson, Colloids Surf., B 37, 71 (2004).
W. Norde and D. Gage, Langmuir 20, 4162 (2004).
L. D. Unsworth, H. Sheardown, and J. L. Brash, Langmuir d21, 1036 (2005).
G. L. Kenausis, J. Voros, D. L. Elbert, N. Huang, R. Hofer, L. Ruiz-Taylor, M. Textor, J. A. Hubbell, and N. D. Spencer, J. Phys. Chem. B 104, 3298 (2000).
J. G. Archambault and J. L. Brash, Colloids Surf., B 33, 111 (2004).
K. L. Prime and G. M. Whitesides, Science 252, 1164 (1991).
K. L. Prime and G. M. Whitesides, J. Am. Chem. Soc. 115, 10174 (1993).
P. Harder, M. Grunze, R. Dahint, G. M. Whitesides, and P. E. Laibinis, J. Phys. Chem. B 102, 426 (1998).
S. Herrwerth, W. Eck, S. Reinhardt, and M. Grunze, J. Am. Chem. Soc. 125, 9359 (2003).
D. V. Vanderah, H. La, J. Naff, V. Silin, and K. A. Rubinson, J. Am. Chem. Soc. 126, 13639 (2004).
J. H. Lee, J. Kopecek and J. D. Andrade, J. Biomed. Mater. Res. 23, 351 (1989).
S. B. Jo and K. Park, Biomaterials 21, 605 (2000).
S. J. Sofia, V. Premnath, and E. W. Merrill, Macromolecules 31, 5059 (1998).
J. Groll, Z. Ademovic, T. Ameringer, D. Klee, and M. Moeller, Biomacromolecules 6, 956 (2005).
J. Benesch, S. Svedhem, S. C. T. Svensson, R. Valiokas, B. Liedberg, and P. Tengvall, J. Biomater. Sci., Polym. Ed. 12, 581 (2001).
Y. Mori, S. Nagaoka, H. Takiuchi, T. Kikuchi, N. Noguchi, H. Tanzawa, and Y. Noishiki, Trans. ASAIO 28, 459 (1982).
S. Nagaoka and A. Nakao, Biomaterials 11, 119 (1990).
Y. H. Sun, A. S. Hoffman, and W. R. Gombotz, Polym. Prepr. (Am. Chem. Soc. Div. Polym. Chem.) 28, 292 (1987).
K. Fujimoto, H. Inoue, and Y. Ikada, J. Biomed. Mater. Res. 27, 1559 (1993).
F. Zhang, E. T. Kang, K. G. Neoh, P. Wang, and K. L. Tan, J. Biomed. Mater. Res. 56, 324 (2001).
W. Feng, R. X. Chen, J. L. Brash, and S. P. Zhu, Macromol. Rapid Commun. 26, 1383 (2005).
F. J. Xu, Y. L. Li, E. T. Kang, and K. G. Neoh, Biomacromolecules 6, 1759 (2005).
H. W. Ma, J. H. Hyun, P. Stiller, and A. Chilkoti, Adv. Mater. (Weinheim, Ger.) 16, 338 (2004).
X. W. Fan, L. J. Lin, J. L. Dalsin, and P. B. Messersmith, J. Am. Chem. Soc. 127, 15843 (2005).
A. L. Lewis, Colloids Surf., B 18, 261 (2000).
V. A. Tegoulia, W. S. Rao, A. T. Kalambur, J. F. Rabolt, and S. L. Cooper, Langmuir 17, 4396 (2001).
K. Ishihara, H. Nomura, T. Mihara, K. Kurita, Y. Iwasaki, and N. Nakabayashi, J. Biomed. Mater. Res. 39, 323 (1998).
H. Kitano, K. Sudo, K. Ichikawa, M. Ide, and K. Ishihara, J. Phys. Chem. B 104, 11425 (2000).
J. R. Lu, E. F. Murphy, T. J. Su, A. L. Lewis, P. W. Stratford, and S. K. Satija, Langmuir 17, 3382 (2001).
E. Ostuni, R. G. Chapman, R. E. Holmlin, S. Takayama, and G. M. Whitesides, Langmuir 17, 5605 (2001).
S. F. Chen, J. Zhang, L. Y. Li, and S. Y. Jiang, J. Am. Chem. Soc. 127, 14473 (2005).
A. Korematsu, Y. Takemoto, T. Nakaya, and H. Inoue, Biomaterials 23, 263 (2002).
K. Kim, C. Kim, and Y. Byun, Biomaterials 25, 33 (2004).
T. Moro, Y. Takatori, K. Ishihara, T. Konno, Y. Takigawa, T. Matsushita, U. I. Chung, K. Nakamura, and H. Kawaguchi, Nat. Mater. 3, 829 (2004).
X. Y. Chen and S. P. Armes, Adv. Mater. (Weinheim, Ger.) 15, 1558 (2003).
R. Iwata, P. Suk-In, V. P. Hoven, A. Takahara, K. Akiyoshi, and Y. Iwasaki, Biomacromolecules 5, 2308 (2004).
W. Feng, J. L. Brash, and S. P. Zhu, J. Polym. Sci., Part A: Polym. Chem. 42, 2931 (2004).
W. Feng, J. L. Brash, and S. P. Zhu, Biomaterials 27, 847 (2006).
W. Feng, S. P. Zhu, K. Ishihara, and J. L. Brash, Langmuir 21, 5980 (2005).
K. Ishihara, T. Ueda, and N. Nakabayashi, Polym. J. (Tokyo, Jpn.) 22, 355 (1990).
X. Jin, Y. Shen, and S. P. Zhu, Macromol. Mater. Eng. 288, 925 (2003).
M. Husseman, E. E. Malmstrom, M. McNamara, M. Mate, D. Mecerreyes, D. G. Benoit, J. L. Hedrick, P. Mansky, E. Huang, T. P. Russell, and C. J. Hawker, Macromolecules 32, 1424 (1999).
I. Y. Ma, E. J. Lobb, N. C. Billingham, S. P. Armes, A. L. Lewis, A. W. Lloyd, and J. Salvage, Macromolecules 35, 9306 (2002).
Density of poly(OEGMA) measured in house.
K. Yamamoto, Y. Miwa, H. Tanaka, M. Sakaguchi, and S. Shimada, J. Polym. Sci., Part A: Polym. Chem. 40, 3350 (2002).
L. Andruzzi, W. Senaratne, A. Hexemer, E. D. Sheets, B. Ilic, E. J. Kramer, B. Baird, and C. K. Ober, Langmuir 21, 2495 (2005).
T. Wu, K. Efimenko, and J. Genzer, J. Am. Chem. Soc. 124, 9394 (2002).
J. Kim and G. A. Somorjai, J. Am. Chem. Soc. 12, 3150 (2003).
A. Halperin, Langmuir 15, 2525 (1999).
S. Pasche, M. Textor, L. Meagher, N. D. Spencer, and H. J. Griesser, Langmuir 21, 6508 (2005).
J. Zhang, L. Y. Li, H. K. Tsao, Y. J. Sheng, S. F. Chen, and S. Y. Jiang, Biophys. J. 89, 158 (2005).
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Feng, W., Zhu, S., Ishihara, K. et al. Protein resistant surfaces: Comparison of acrylate graft polymers bearing oligo-ethylene oxide and phosphorylcholine side chains. Biointerphases 1, 50–60 (2006). https://doi.org/10.1116/1.2187495