Diels-Alder reaction for the selective immobilization of protein to electroactive self-assembled monolayers

Journal of the American Chemical Society

Volumn 121, Issue 17, 1999, Pages 4286-4287

  Yousaf, Muhammad N ^a   Mrksich, Milan ^a  

^a UNIVERSITY OF CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINE; BIOTIN; STREPTAVIDIN;

ANALYTIC METHOD; ARTICLE; ELECTROCHEMISTRY; MONOLAYER CULTURE; POLYMERIZATION; POTENTIOMETRY; PROTEIN IMMOBILIZATION;

EID: 0033526361     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja983529t     Document Type: Article

References (24)

1. Schuna, M.; Heller, R. A.; Theriault, T. P.; Konrad, K.; Lachenmeier, E.; Davis, R. W. Trends Biotechnol. 1998, 16, 301-306. Mrksich, M. Curr. Opin. Colloid Interface Sci. 1997, 2, 83-88. Hermanson, G. T. Bioconjugate Techniques; Academic Press: New York, 1996.
2. Schuna, M.; Heller, R. A.; Theriault, T. P.; Konrad, K.; Lachenmeier, E.; Davis, R. W. Trends Biotechnol. 1998, 16, 301-306. Mrksich, M. Curr. Opin. Colloid Interface Sci. 1997, 2, 83-88. Hermanson, G. T. Bioconjugate Techniques; Academic Press: New York, 1996.
3. Schuna, M.; Heller, R. A.; Theriault, T. P.; Konrad, K.; Lachenmeier, E.; Davis, R. W. Trends Biotechnol. 1998, 16, 301-306. Mrksich, M. Curr. Opin. Colloid Interface Sci. 1997, 2, 83-88. Hermanson, G. T. Bioconjugate Techniques; Academic Press: New York, 1996.
4. Green, N. M. Methods Enzymol. 1990, 184, 51-67.
5. (a) Wilbur, D. S.; Hamlin, D. K.; Pathare, P. M.; Weerawarna, S. A. Bioconjugate Chem. 1997, 8, 572-584.
6. (b) Horton, R. C.; Herne, T. M.; Myles, D. C. J. Am. Chem. Soc. 1997, 119, 12980-12981.
7. (c) Sigal, G. B.; Bamdad, C.; Barberis, A. A.; Strominger, J.; Whitesides, G. M. Anal. Chem. 1996, 98, 490-497.
8. HQ is the fraction of alkanethiolates in the monolayer that present HQ and is determined by integrating the waves in cyclic voltammograms of the monolayer.
9. For previous reports of the electrochemistry of SAMs presenting HQ groups, see: Hickman, J. J.; Ofer, D.; Laibinis, P. E.; Whitesides, G. M.; Wrighton, M. S. Science 1991, 252, 688-691. Ye, S.; Yashiro, A.; Sato, Y.; Uosaki, K. J. Chem. Soc., Faraday Trans. 1996, 92, 3813-3821.
10. For previous reports of the electrochemistry of SAMs presenting HQ groups, see: Hickman, J. J.; Ofer, D.; Laibinis, P. E.; Whitesides, G. M.; Wrighton, M. S. Science 1991, 252, 688-691. Ye, S.; Yashiro, A.; Sato, Y.; Uosaki, K. J. Chem. Soc., Faraday Trans. 1996, 92, 3813-3821.
11. Cyclic voltammetry was performed with a Bioanalytical Systems CV-50W potentiostat using a cell with the gold/SAM as the working electrode, platinum wire as the counter electrode, and Ag/AgCl as the reference electrode.
12. The tautomerization of the D-A adduct, which would yield a redox-active quinone, requires strongly acidic or basic conditions and does not proceed under the conditions employed here. See: Meinwald, J.; Wiley: G. A. J. Am. Chem. Soc. 1958, 80, 3667-3670.
13. 2O proceeded at least 300 times faster than did the interfacial reaction. We are exploring the basis for the difference in rates.
14. Spinke, J.; Liley, M.; Guder, H. J.; Angermaier, L.; Knoll, W. Langmuir 1993, 9, 1821-1825. Spinke, J.; Liley, M.; Schmitt, F. J.; Guder, H. J.; Angermaier, L.; Knoll, W. J. Chem. Phys. 1993, 99, 7012-7019.
15. Spinke, J.; Liley, M.; Guder, H. J.; Angermaier, L.; Knoll, W. Langmuir 1993, 9, 1821-1825. Spinke, J.; Liley, M.; Schmitt, F. J.; Guder, H. J.; Angermaier, L.; Knoll, W. J. Chem. Phys. 1993, 99, 7012-7019.
16. Mrksich, M.; Whitesides, G. M. In Chemistry and Biological Applications of Polyethylene Glycol; ACS Symposium Series 680, American Chemical Society: Washington, DC, 1997; p 361 and references therein.
17. 1H NMR spectra. Details will be described in a subsequent full report.
18. We used a chemical oxidant because the instrument for SPR is not compatible with electrochemistry. The ability to use chemical oxidants and reductants to interconvert the HQ and Q also expands the utility of this method to nonconducting substrates.
19. For examples of the use of SPR to measure the association of proteins with monolayers, see: Mrksich, M.; Grunwell, J. R.; Whitesides, G. M. J. Am. Chem. Soc. 1995, 117, 12009-12010. Houseman, B. T.; Mrksich, M. Angew. Chem., Int. Ed. 1999, 38, 782-785.
20. For examples of the use of SPR to measure the association of proteins with monolayers, see: Mrksich, M.; Grunwell, J. R.; Whitesides, G. M. J. Am. Chem. Soc. 1995, 117, 12009-12010. Houseman, B. T.; Mrksich, M. Angew. Chem., Int. Ed. 1999, 38, 782-785.
21. The magnitude of change in θ when streptavidin is flowed over the monolayer presenting quinone and glycol groups is greater than that observed with monolayers presenting only glycol groups and shows that the protein adsorbs to the mixed monolayer. This adsorption does not result in immobilization of streptavidin, since it is weak and rapidly reversible when the protein-containing solution is replaced with buffer.
22. SAMs are currently the best available class of model substrates for studies in biointerfacial science. For reviews, see: Mrksich, M. Cell. Mol. Life Sci. 1998, 54, 653-58. Mrksich, M.; Whitesides, G. M. Annu. Rev. Biophys. Biomol. Struct. 1996, 25, 55-78.
23. SAMs are currently the best available class of model substrates for studies in biointerfacial science. For reviews, see: Mrksich, M. Cell. Mol. Life Sci. 1998, 54, 653-58. Mrksich, M.; Whitesides, G. M. Annu. Rev. Biophys. Biomol. Struct. 1996, 25, 55-78.
24. Hodneland, C. H.; Mrksich, M. Langmuir 1997, 13, 6001-6003.