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Formation of surface-grafted polymeric amphiphilic coatings comprising ethylene glycol and fluorinated groups and their response to protein adsorption
Biointerphases volume 4, pages FA33–FA44 (2009)
Abstract
Amphiphilic polymer coatings were prepared by first generating surface-anchored polymer layers of poly(2-hydroxyethyl methacrylate) (PHEMA) on top of flat solid substrates followed by postpolymerization reaction on the hydroxyl terminus of HEMA’s pendent group using three classes of fluorinating agents, including organosilanes, acylchlorides, and trifluoroacetic anhydride (TFAA). The distribution of the fluorinated groups inside the polymer brushes was assessed by means of a suite of analytical probes, including contact angle, ellipsometry, infrared spectroscopy, atomic force microscopy, and near-edge x-ray absorption fine structure spectroscopy. While organosilane modifiers were found to reside primarily close to the tip of the brush, acylchlorides penetrated deep inside PHEMA thus forming random copolymers P(HEMA-co-fHEMA). The reaction of TFAA with the PHEMA brush led to the formation of amphiphilic diblocks, PHEMA-b-P(HEMA-co-fHEMA), whose bottom block comprised unmodified PHEMA and the top block was made of P(HEMA-co-fHEMA) rich in the fluorinated segments. This distribution of the fluorinated groups endowed PHEMA-b-P(HEMA-co-fHEMA) with responsive properties; while in hydrophobic environment P(HEMA-co-fHEMA) segregated to the surface, when in contact with a hydrophilic medium, PHEMA partitioned at the brush surface. The surface activity of the amphiphilic coatings was tested by studying the adsorption of fibrinogen (FIB). While some FIB adsorption occurred on most coatings, the ones made by TFAA modification of PHEMA remained relatively free of FIB.
References
M. Mrksich and G. M. Whitesides, Annu. Rev. Biophys. Biomol. Struct. 25, 55 (1996).
J.Genzer and K.Efimenko, Biofouling 22, 339 (2006) and references therein.
S. Krishnan, C. J. Weinman, and C. K. Ober, J. Mater. Chem. 18, 3405 (2008).
S. Herrwerth, W. Eck, S. Reinhardt, and M. Grunze, J. Am. Chem. Soc. 125, 9359 (2003).
S. Satzl, C. Henn, P. Christoph, P. Kurz, U. Stampfl, S. Stampfl, F. Thomas, B. Radeleff, I. Berger, M. Grunze, and G. M. Richter, Invest. Radiol. 42, 303 (2007).
S. Chen, J. Zheng, L. Li, and S. Jiang, J. Am. Chem. Soc. 127, 14473 (2005).
G. Cheng, Z. Zhang, S. Chen, J. D. Bryers, and S. Jiang, Biomaterials 28, 4192 (2007).
L. K. Ista, M. E. Callow, J. A. Finlay, S. E. Coleman, A. C. Bolasco, R. H. Simons, J. A. Callow, and G. P. López, Appl. Environ. Microbiol. 70, 4151 (2004).
D. Gan, A. Mueller, K. L. Wooley, J. Polym. Sci., Part A: Polym. Chem. 41, 3531 (2003).
C. S. Gudipati, J. A. Finlay, J. A. Callow, M. E. Callow, and K. L. Wooley, Langmuir 21, 3044 (2005).
C. S. Gudipati, C. M. Greenlieaf, J. A. Johnson, P. Pornpimol, K. L. Wooley, J. Polym. Sci., Part A: Polym. Chem. 42, 6193 (2004).
S. Krishnan, R. Ayothi, A. Hexemer, J. A. Finlay, K. E. Sohn, R. Perry, C. K. Ober, E. J. Kramer, M. E. Callow, J. A. Callow, and D. A. Fischer, Langmuir 22, 5075 (2006).
S. Schilp, A. Kueller, A. Rosenhahn, M. Grunze, M. E. Pettitt, M. E. Callow, and J. A. Callow, BioInterphases 2, 143 (2007).
K. Matyjaszewski et al., Macromolecules, 32, 8716 (1999).
K. L. Robinson, M. A. Khan, M. V. de Paz Banez, X. S. Wang, and S. P. Ames, Macromolecules 34, 3155 (2001).
A. Ulman, Chem. Rev. (Washington, D.C.) 96, 1533 (1996).
F. Schreiber, Prog. Surf. Sci. 65, 151 (2000).
C. G. L. Khoo, J. B. Lando, and H. Ishida, J. Polym. Sci., Part B: Polym. Phys. 28, 213 (1990).
X. M. Deng, E. J. Castillo, and J. M. Anderson, Biomaterials 7, 247 (1986).
S. Spange, U. Eismann, S. Hohne, and E. Langhammer, Macromol. Symp. 126, 223 (1998).
E. L. Brantley and G. K. Jennings, Macromolecules 37, 1476 (2004).
M. R. Bantz, E. L. Brantley, R. D. Weinstein, J. Moriarty, and G. K. Jennings, J. Phys. Chem. B 108, 9787 (2004).
E. L. Brantley, T. C. Holmes, and G. K. Jennings, J. Phys. Chem. B 108, 16077 (2004).
G. K. Jennings and E. L. Brantley, Adv. Mater. (Weinheim, Ger.) 16, 1983 (2004).
E. L. Brantley, T. C. Holmes, and G. K. Jennings, Macromolecules 38, 9730 (2005).
T. I. Valdes, W. Ciridon, B. D. Ratner, and J. D. Bryers, Biomaterials 29, 1356 (2008).
L. Guicai, S. Xiaoli, Y. Ping, Z. Ansha, and H. Nan, Solid State Ionics 179, 932 (2008).
J. Brandrup, E. H. Immergut, E. A. Grulke, and D. Bloch, Polymer Handbook, 4th ed. (Wiley, New York, 2005), pp. VI/576.
A. Ulman, An Introduction to Ultrathin Organic Films: From Langmuir-Blodgett to Self-Assembly (Academic, Boston, 1991), p.4422.
The probing depth of XPS, d, is defined as 3λ sin α, where λ is the electron mean free path and α is the take-off angle. Electron mean free paths for the compounds studied are all ≈ 3 nm, as estimated from the contributions of individual electron mean free paths of C (=3.3 nm), O (=3.0 nm), F (=2.7 nm), and Si (=3.6 nm) (J. C. Vickerman, Surface Analysis: The Principle Techniques (Wiley, Chichester, 1997; (D. J. O’Connor, B. A. Sexton, and R. St. C. Smart, Surface Analysis Methods in Materials Science, 2nd ed. (Springer, Berlin, 2003) and the atomic percentage of each element in the sample determined at α =90°.
J. Stöhr, NEXAFS Spectroscopy (Springer-Verlag, Berlin, 1992).
J. Genzer, K. Efimenko, and D. A. Fischer, Langmuir 18, 9307 (2002).
Y. K. Jhon, J. J. Semler, and J. Genzer, Macromolecules 41, 6719 (2008).
S. Diamanti, S. Arifuzzaman, A. Elsen, J. Genzer, and R. A. Vaia, Polymer 49, 3770 (2008).
E. P. K. Currie, J. van der Gucht, O. V. Borisov, and M. A. Cohen Stuart, Langmuir 14, 5740 (1998).
E. P. K. Currie, G. J. Fleer, M. A. Cohen Stuart, and O. V. Borisov, Eur. Phys. J. E 1, 27 (2000).
R. A. Gage, E. P. K. Currie, and M. A. Cohen Stuart, Macromolecules 34, 5078 (2001).
Z. Liu, K. Pappacena, J. Cerise, J. Kim, C. J. Durning, B. O’Shaughnessy, and R. Levicky, Nano Lett. 2, 219 (2002).
J. U. Kim and B. O’Shaughnessy, Phys. Rev. Lett. 89, 238301 (2002).
R. R. Bhat and J. Genzer, Appl. Surf. Sci. 252, 2549 (2006).
S.Diamanti, S.Arifuzzaman, J. Genzer, and R. A.Vaia, ACS Nano (in press).
We estimate that σPHEMA ≈0.45 nm−2, based on previous report, in which the grafting density was measured directly. In both cases the procedure leading to the formation of the initiator SAM was identical.
A rough correlation between the brush dry thickness (h) and molecular weight of the brush can be established (M=1200h, where h is in nanometers), as detailed in M. R. Tomlinson and J. Genzer, Langmuir 21, 11552 (2005).
Note that the contact angle of PHEMA brushes may vary by as much as 15° depending on the humidity present. “Bone dry” PHEMA layers typically exhibit contact angles of ≈ 55°. When moisture is present in the air, PHEMA absorbs and becomes more hydrophilic.
M. Callies and D. Quéré, Soft Matter 1, 55 (2005).
A. Marmur, Langmuir 22, 1400 (2006).
K. E. Sohn, J. Dimitriou, J.Genzer, D. A.Fischer, C. J. Hawker, and E. J. Kramer, Langmuir (in press).
S. Turgman-Cohen, D. A. Fischer, P. K. Kilpatrick, and J. Genzer (submitted).
E. Triantaphyllopoulos and D. C. Triantaphyllopoulos, Biochem. J. 105, 393 (1967).
C. E. Halland H. S. Slayter, J. Biophys. Biochem. Cytol. 5, 11 (1959).
J. M. Grunkemeier, W. B. Tsai, C. D. McFarland, and T. A. Horbett, Biomaterials 21, 2243 (2000).
S. Spange, U. Eismann, S. Hohne, and E. Langhammer, Macromol. Symp. 126, 223 (1998).
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Arifuzzaman, S., Özçam, A.E., Efimenko, K. et al. Formation of surface-grafted polymeric amphiphilic coatings comprising ethylene glycol and fluorinated groups and their response to protein adsorption. Biointerphases 4, FA33–FA44 (2009). https://doi.org/10.1116/1.3114502
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DOI: https://doi.org/10.1116/1.3114502