A survey of structure-property relationships of surfaces that resist the adsorption of protein

Langmuir

Volumn 17, Issue 18, 2001, Pages 5605-5620

  Ostuni, Emanuele ^a   Chapman, Robert G ^a   Holmlin, R Erik ^a   Takayama, Shuichi ^a   Whitesides, George M ^a  

^a HARVARD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FUNCTIONAL GROUPS;

ADSORPTION; AMINES; CHARACTERIZATION; DERIVATIVES; ELLIPSOMETRY; HYDROGEN BONDS; HYDROPHILICITY; MONOLAYERS; PROTEINS; SOLUTIONS; SURFACE PLASMON RESONANCE; SYNTHESIS (CHEMICAL);

SELF ASSEMBLY;

EID: 0035807149     PISSN: 07437463     EISSN: None     Source Type: Journal    
DOI: 10.1021/la010384m     Document Type: Review

References (77)

1. Ratner, B.D.; Hoffmann, F.J.; Schoen, J.E.; Lemons, F. Biomaterials Science. An Introduction to Materials in Medicine; Academic Press: New York, 1996.
2. Chen, C.S.; Mrksich, M.; Huang, S.; Whitesides, G.M.; Ingber, D.E. Science 1997, 276, 1425-1428.
3. Niklason, L.E.; Gao, J.; Abbott, W.M.; Hirschi, K.K.; Houser, S.; Marini, R.; Langer, R. Science 1999, 284, 489-493.
4. Manz, A.; Becker, H. Microsystem Technology in Chemistry and Life Sciences; Springer-Verlag: Berlin, Germany, 1998.
5. Santini, J.T.; Cima, M.J.; Langer, R. Nature 1999, 397, 335-338.
6. Fu, K.; Klibanov, A.M.; Langer, R. Nat. Biotechnol. 2000, 18, 24-25.
7. Macbeath, G.; Schreiber, S.L. Science 2000, 289, 1760-1763.
8. Whitney, M.; Rockenstein, E.;antin, G.; Knapp, T.; Zlokarnik, G.; Sanders, P.; Durick, K.; Craig, F.F.; Negulescu, P.A. Nat. Biotechnol. 1998, 16, 1329-1333.
9. Chapman, R.G.; Ostuni, E.; Takayama, S.; Holmlin, R.E.; Yan, L.; Whitesides, G.M. J. Am. Chem. Soc. 2000, 122, 8303-8304.
10. Holmlin, R.E.; Chen, X.; Chapman, R.G.; Takayama, S.T.;Whitesides, G.M. Langmuir 2001, 17 (9), 2841-2850.
11. Luk, Y.-Y.; Kato, M.; Mrksich, M. Langmuir 2000, 16, 9604-9608.
12. Harris, J.M.; Zalipsky, S. Poly(ethylene glycol): Chemistry and Biological Applications; American Chemical Society: Washington, D.C., 1997.
13. Jeon, S.I.; Lee, L.H.; Andrade, J.D.: de Gennes, P.G. J. Colloid Interface Sci. 1991. 142, 149 158.
14. McPherson, T.; Kidane, A.; Szleifer, I.; Park, K. Langmuir 1998, 14, 176-186.
15. Jenney, C.R.; Anderson, J.M. J. Biomed. Mater. Res. 1999, 44, 206-216.
16. Deible, C.R.; Petrosko, P.; Johnson, P.C.; Beckman, E.J.; Russell, A.J.; Wagner, W.R. Biomaterials 1998, 19, 1885-1893.
17. Crouzet, C.; Decker, C.; Marchal, J. Makromol. Chem. 1976. 277, 145-157.
18. Hamburger, R.; Azaz, E.; Donbrow, M. Pharm. Acta Helv. 1975. 50, 10-17.
19. Gerhardt, W.; Martens, C.Z. Chem. 1985, 25, 143.
20. Talarico, T.; Swank, A.; Privalle, C. Biochem. Biophys. Res. Commun. 1998, 250, 354-358.
21. Herold, D.A.; Keri, K.; Bruns, D.E. Biochem. Pharm. 1989, 38, 73-76.
22. Chapman, R.G.; Ostuni, E.; Yah, L.; Whitesides, G.M. Langmuir 2000, 16, 6927-6936.
23. Prime, K.L.; Whitesides, G.M. J. Am. Chem. Soc. 1993, 115, 10714-10721.
24. Prime, K.L.; Whitesides, G.M. Science 1991, 252, 1164-1167.
25. Deng, L.; Mrksich, M.; Whitesides, G.M. J. Am. Chem. Soc. 1996, 118, 5136-5137.
26. Soderquist, M.E.; Walton, A.G. J. Colloid Interface Sci. 1980, 75, 386-397.
27. Hook, F.; Rodahl, M.; Kasemo, B.; Brzezinski, P. Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 12271-12276.
28. Ramsden, J.J.Q. Rev. Biophys. 1993, 27, 41-105.
29. Kingshott, P.; Griesser, H. J. Curt. Opin. Solid State Mater. Sci. 1999, 4, 403-412.
30. Schaaf, P.; Voegel, J.C.; Senger, B. Ann. Phys. Paris 1998, 23, 1-5.
31. Talbot, J.; Tarjus, G.; Van Tassel, P.R.; Viot, P. Colloid Surf. A: Physicochem. Eng. Aspects 2000, 165, 287-324.
32. Andrade, J.D.; Hlady, V. Adv. Polym. Sci. 1986, 79, 1-63.
33. Jeon, S.I.; Andrade, J.D. J. Colloid Interface Sci. 1991, 142, 159-165.
34. Szleifer, I. Curr. Opin. Solid State Mater. Sci. 1997, 2, 337-344.
35. Szleifer, I. Physica A 1997, 244, 370-388.
36. Besseling, N.A.M. Langmuir 1997, 13, 2113-2122.
37. Satulovsky, J.; Carignano, M.A.; Szleifer, I. Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 9037-9041.
38. Wang, R.L.C.; Kreuzer, H.J.; Grunze, M. J. Phys. Chem. B 1997, 101, 9767-9773.
39. Harder, P.; Grunze, M.; Dahint, R.; Whitesides, G.M.; Laibinis, P.E. J. Phys. Chem. B 1998, 102, 426-436.
40. Feldman, K.; Hahner, G.; Spencer, N.D.; Harder, P.; Grunze, M. J. Am. Chem. Soc. 1999, 121, 10134-10141.
41. Pertsin, A.J.; Grunze, M. Langmuir 2000, 16, 8829-8841.
42. Wang, R.L.C.; Kreuzer, H.J.; Grunze, M.; Pertsin, A. J. PCCP Phys. Chem. Chem. Phys. 2000, 2, 1721-1727.
43. Zolk, M.; Eisert, F.; Pipper, J.; Herrwerth, S.; Eck, W.; Buck, M.; Grunze, M. Langmuir 2000, 16, 5849-5852.
44. Wang, R.L.C.; Kreuzer, H.J.; Grunze, M. PCCP Phys. Chem. Chem. Phys. 2000, 2, 3613-3622.
45. Jordan, C.E.; Frey, B.L.; Kornguth, S.; Corn, R.M. Langmuir 1994, 10, 3642-3648.
46. Thiel, A.J.; Frutos, A.G.; Jordan, C.E.; Corn, R.M.; Smith, L.M. Anal. Chem. 1997, 69, 4948-4956.
47. Jordan, C.E.; Corn, R.M. Anal. Chem. 1997, 69, 1449-1456.
48. Mrksich, M.; Grunwell, J.R.; Whitesides, G.M. J. Am. Chem. Soc. 1995, 117, 12009-12010.
49. Sigal, G.B.; Bamdad, C.; Barberis; A.; Strominger, J.; Whitesides, G.M. Anal. Chem. 1996, 68, 490-497.
50. Whitesides, G.M.; Laibinis, P.E. Langmuir 1990, 6, 87-96.
51. Bain, C.D.; Whitesides, G.M. Science 1988, 240, 62-63.
52. Raether, H. In Physics of Thin Films; Hass, G., Francombe, M., Hoffman, R., Eds.; Academic Press: New York, 1977; Vol. 9, pp 145-261.
53. Niemz, A.; Jeoung, E.; Boal, A.K.; Deans, R.; Rotello, V.M. Langmuir 2000, 16, 1460-1462.
54. Lahiri, J.; Isaacs, L.; Tien, J.; Whitesides, G.M. Anal. Chem. 1999, 71, 777-790.
55. Horton, R.C.; Herne, T.M.; Myles, D.C. J. Am. Chem. Soc. 1997, 119, 12980-12981.
56. Yah, L.; Marzolin, C.; Terfort, A.; Whitesides, G.M. Langmuir 1997, 13, 6704-6712.
57. Singhvi, R.; Kumar, A.; Lopez, G.P.; Stephanopolous, G.N.; Wang, D.I.C.; Whitesides, G.M.; Ingber, D.E. Science 1994, 264, 696-698.
58. The molar concentration of lysozyme is 20 times greater than that of fibrinogen for solutions at 1 mg/mL. We used these concentrations to simplify the comparison with previously reported data on the adsorption of these proteins onto SAMs. Fibrinogen did not dissolve in buffer to form a 20 mg/mL solution. On the other hand, a 0.05 mg/mL solution of lysozyme would make the adsorption process very slow and most likely limited by mass transport.
59. We are uncertain about the drastic differences between the kinetics of the adsorption of fibrinogen and lysozyme displayed in Figure 2. We speculate that they are caused by electrostatic effects.
60. Although the structure, thickness, and index of refraction of the adsorbed layer depend on the conformation of the protein on the surface, the actual quantity of protein that adsorbs onto the alkyl-terminated surface almost certainly represents a complete monolayer.
61. Mrksich, M.; Sigal, G.B.; Whitesides, G.M. Langmuir 1995, 11, 4383-4385.
62. Sigal, G.B.; Mrksich, M.; Whitesides, G.M. J. Am. Chem. Soc. 1998, 120, 3464-3473.
63. Szleifer, I. Biophys. J. 1997, 72, 595-612.
64. Frensdorf, H.K. J. Am. Chem. Soc. 1971, 93, 600-606.
65. Merz, A.; Gromann, L.; Karl, A.; Parkanyi, L.; Schneider, O. Eur. J. Org. Chem. 1998, 403, 3-408.
66. Patti, K.; Pawar, R. J. Phys. Chem. B 1999, 103, 2256-2261.
67. Holland, N.B.; Qui, S.X.; Ruegsegger, M.; Marchant, R.E. Nature 1998, 392, 799-801.
68. We have not tried to generate a surface terminated with mannose groups such as that used by Mrksich because we could not easily create a mixed SAM that contained an O-linked mannitol derivative.
69. Mrksich, M. Department of Chemistry, University of Chicago. Personal communication, 2001.
70. The reactivity of the amino group in entry 38 is probably lowered significantly by the presence of the alkene, which causes a low yield in this reaction with the anhydride surface.
71. We chose to measure the contact angle of water in cyclooctane for several reasons. (i) Most evidence points to the crucial role played by water in the mechanism of resistance; hence, it was most appropriate to measure the interaction of water with the surfaces. (ii) Values of the contact angle of water in cyclooctane On other SAMs are available from other groups. (iii) Theoretically, provided that the solvents do not cause drastic changes in the structure of the SAMs, the contact angle of water in cyclooctane corresponds to 180° - the contact angle of cyclooctane in water.
72. Ostuni, E.; Chapman, R.G.; Liang, M.N.; Meluleni, G.; Pier, G.; Ingber, D.E.; Whitesides, G.M. 2001, Langmuir, in press.
73. Claesson, P.M. In Biopolymers at Interfaces; Malmsten, M., Ed.; Marcel Dekker: New York, 1998; Vol. 75, pp 281-320.
74. Rau, D.C.; Parsegian, V.A. Science 1990, 249, 1278-1281.
75. Chapman, R.G.; Ostuni, E.; Liang, M.N.; Meluleni, G.; Kim, E.; Yan, L.; Pier, G.; Warren, H.S.; Whitesides, G.M. Langmuir 2001, 17, 1225-1233.
76. Saari, W.S.; Schwering, J.E.; Lyle, P.A.; Smith, S.J.; Engelhardt, E.L. J. Med. Chem. 1990, 33, 97-101.
77. Cravey, M.J.; Kohn, H. J. Am. Chem. Soc. 1980, 102, 3928-3939.