Biomolecular surfaces that release ligands under electrochemical control [12]

Journal of the American Chemical Society

Volumn 122, Issue 17, 2000, Pages 4235-4236

  Hodneland, Christian D ^a   Mrksich, Milan ^a  

^a UNIVERSITY OF CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOTIN;

ELECTROCHEMISTRY; LETTER; MOLECULAR INTERACTION; PROTEIN BINDING; SURFACE PLASMON RESONANCE;

EID: 0034600254     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja000419p     Document Type: Letter

References (23)

1. (a) Mrksich, M.; Dike, L. E.; Tien, J. Y.; Ingber, D. E.; Whitesides, G. M. Exp. Cell Res. 1997, 235, 305-313.
2. (b) Chen, C. S.; Mrksich, M.; Huang, S.; Whitesides, G. M.; Ingber, D. E. Science 1997, 276, 1345-1347.
3. (a) Roberts, C.; Chen, C. S.; Mrksich, M.; Martichonok, V.; Ingber, D. E.; Whitesides, G. M. J. Am. Chem. Soc. 1998, 120, 6548-6555.
4. (b) Houseman, B. T.; Mrksich, M. J. Org. Chem. 1998, 120, 6548-6555.
5. Bamdad, C. Biophys. J. 1998, 75, 1997-2003.
6. Early examples of materials with dynamic function include: (a) Lau, A. N. K.; Miller, L. L. J. Am. Chem. Soc. 1983, 105, 5271-5277. (b) Ding, Z.; Long, C. J.; Hayashi, Y.; Bulmus, E. V.; Joffman, A. S.; Stayton, P. S. Bioconjugate Chem. 1999, 10, 395-400.
7. Early examples of materials with dynamic function include: (a) Lau, A. N. K.; Miller, L. L. J. Am. Chem. Soc. 1983, 105, 5271-5277. (b) Ding, Z.; Long, C. J.; Hayashi, Y.; Bulmus, E. V.; Joffman, A. S.; Stayton, P. S. Bioconjugate Chem. 1999, 10, 395-400.
8. Yousaf, M. N.; Mrksich, M. J. Am. Chem. Soc. 1999, 121, 4286-4287.
9. (a) Carpino, L. A.; Triolo, S. A.; Berglund, R A. J. Org. Chem. 1989, 54, 3303-3310.
10. (b) Wang, B.; Liu, S.; Borchardt, R. T. J. Org. Chem. 1995, 60, 539-543.
11. (c) Zheng, A.; Shan, D.; Wang, B. J. Org. Chem. 1999, 64, 156-161.
12. Milstien, S.; Cohen, L. A. J. Am. Chem. Soc. 1972, 94, 9158-9165.
13. Mrksich, M.; Whitesides, G. M. ACS Symp. Ser. Chem. Biol. Appl. Polyethylene Glycol 1997, 680, 361-373.
14. Bulk electrolysis was performed under un argon atmosphere using a BAS CV-50W potentiostat in a standard cell with a vitreous carbon working electrode of large surface area, a coiled platinum wire counter electrode, and a Ag/AgCl/KCl reference electrode.
15. 13C NMR and TLC.
16. For examples of the use of SPR to measure biospecific association of proteins with SAMs, see: (a) Houseman, B. T.; Mrksich, M. Angew. Chem., Int. Ed. 1999, 38, 782-785. (b) Mrksich, M.; Grunwell, J. R.; Whitesides, G. M. J. Am. Chem. Soc. 1995, 117, 12009-12010. (c) Spinke, J.; Liley, M.; Guder, H. J.; Angermaier, L.; Knoll, W. Langmuir 1993, 9, 1821-1825.
17. For examples of the use of SPR to measure biospecific association of proteins with SAMs, see: (a) Houseman, B. T.; Mrksich, M. Angew. Chem., Int. Ed. 1999, 38, 782-785. (b) Mrksich, M.; Grunwell, J. R.; Whitesides, G. M. J. Am. Chem. Soc. 1995, 117, 12009-12010. (c) Spinke, J.; Liley, M.; Guder, H. J.; Angermaier, L.; Knoll, W. Langmuir 1993, 9, 1821-1825.
18. For examples of the use of SPR to measure biospecific association of proteins with SAMs, see: (a) Houseman, B. T.; Mrksich, M. Angew. Chem., Int. Ed. 1999, 38, 782-785. (b) Mrksich, M.; Grunwell, J. R.; Whitesides, G. M. J. Am. Chem. Soc. 1995, 117, 12009-12010. (c) Spinke, J.; Liley, M.; Guder, H. J.; Angermaier, L.; Knoll, W. Langmuir 1993, 9, 1821-1825.
19. 1H NMR and MS spectra.
20. 2). Experiments show a change in θ immediately following protein injection due to differences in refractive index between the two solutions.
21. Electrochemistry was performed in buffered water (PBS, pH 7.4) using the gold substrate as the working electrode, a platinum wire as the counter electrode, and a Ag/AgCl/KCl reference electrode - prior to mounting the substrate in a cartridge for analysis by SPR.
22. Ellipsometric characterization of a monolayer that presented the biotin quinone propionic ester at a density of 25% (to increase signal contrast) showed that the thickness decreased by 5 Å after electrochemical treatment, consistent with release of biotin from the surface. Grazing-angle FTIR spectra were inconclusive, presumably because of the disordered structure of the oligo-(ethylene glycol) groups and the biotin quinone propionic ester groups.
23. The use of more extreme potentials (-1100 mV for 5 min) gave mono-layers that were no longer inert to non-specific protein adsorption (Figure 2E). and lower potentials (-600 mV for 3 min) gave incomplete cleavage of biotin.