Molecular recognition between genetically engineered streptavidin and surface-bound biotin

Journal of the American Chemical Society

Volumn 121, Issue 27, 1999, Pages 6469-6478

  Pérez Luna, Víctor H ^a   O'Brien, Michael J ^b   Opperman, Kimberly A ^b   Hampton, Philip D ^b   López, Gabriel P ^a,b   Klumb, Lisa A ^c   Stayton, Patrick S ^c  

^a University of New Mexico   (United States)

^b UNIVERSITY OF NEW MEXICO   (United States)

^c University of Washington   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; BIOTIN; GOLD; HYDROXYTHIOL; MUTANT PROTEIN; STREPTAVIDIN; THIOAMIDE; TRYPTOPHAN; TYROSINE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING KINETICS; CHEMICAL STRUCTURE; CONCENTRATION RESPONSE; DESORPTION; GENETIC ENGINEERING; METAL BINDING; MOLECULAR DYNAMICS; MOLECULAR RECOGNITION; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; REACTION ANALYSIS;

EID: 0033554016     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja983984p     Document Type: Article

References (42)

1. Chaiet, L.; Wolf, F. J. Arch. Biochem. Biophys. 1964, 106, 1-5.
2. Green, N. M. Adv. Protein Chem. 1975, 29, 85-133.
3. Weber, P. C.; Ohlendorf, D. H.; Wendoloski, J. J.; Salemme, F. R. Science 1989, 243, 85-88.
4. Hermanson, G. T.; Mallia, A. K.; Smith, P. K. Immobilized Affinity Ligand Techniques; Academic Press: San Diego, CA, 1992.
5. Bayer, E. A.; Wilchek, M. J. Chromatogr. 1990, 510, 3-11.
6. Diamandis, E. P.; Christopoulos, T. K. Clin. Chem. 1991, 37, 625-636.
7. Wilchek, M.; Bayer, E. A. Avidin-Biotin Technology. In Methods in Enzymology 1990, 184, 5-13, 14-45.
8. Oehr, P.; Westermann, J.; Biersack, H. J. J. Nucl. Med. 1988, 29, 728-729.
9. Hnatowich, D. J.; Virzi, F.; Rusckowski, M. J. Nucl. Med. 1987, 28, 1294-1302.
10. Kalofonos, H. P.; Rusckowski, M.; Siebecker, D. A.; Sivolapenko, G. B.; Snook, D.; Lavender, J. P.; Epenetos, A. A.; Hnatowich, D. J. J. Nucl. Med. 1990, 31, 1791-1796.
11. Alvarez-Diez, T. M.; Polihronis, J.; Reilly, R. M. Nucl. Med. Biol. 1996, 23, 459-466.
12. Rosebrough, S. F.; Hashmi, M. J. Pharmacol. Exp. Ther. 1996, 276, 770-775.
13. Ogiharaumeda, I.; Sasaki, T.; Toyama, H.; Oda, K.; Senda, M.; Nishigori, H. Cancer Res. 1994, 54, 463-467.
14. Rusckowski, M.; Paganelli, G.; Hnatowich, D. J.; Magnani, P.; Virzi, F.; Fogarasi, M.; Dileo, C.; Sudati, F.; Fazio, F. J. Nucl. Med. 1996, 37, 1655-1662.
15. Vanosdol, W. W.; Sung, C.; Dedrick, R. L.; Weinstein, J. N. J. Nucl. Med. 1993, 34, 1552-1564.
16. Figge, J.; Bakst, G.; Weiheit, D.; Solls, O.; Ross, J. S. Am. J. Pathol. 1991, 139, 1213-1219.
17. Emans, N.; Biwersi, J.; Verkman, A. S. Biophys. J. 1995, 69, 716-728.
18. Haussling, L.; Ringsdorf, H.; Schmitt, F. J.; Knoll, W. Langmuir 1991, 7, 1837-1840.
19. Schmitt, F. J.; Haussling, L.; Ringsdorf, H.; Knoll, W. Thin Solid Films 1992, 210, 815-817.
20. Spinke, J.; Liley, M.; Schmitt, F. J.; Guder, H. J.; Angermaier, L.; Knoll, W. J. Chem. Phys. 1993, 99, 7012-7019.
21. Haussling, L.; Knoll, W.; Ringsdorf, H.; Schmitt, F. J.; Yang, J. L. Makromol. Chem., Macromol. Symp. 1991, 46, 145-155.
22. Haussling, L.; Michel, B.; Ringsdorf, H.; Rohrer, H. Angew. Chem., Int. Ed. Engl. 1991, 30, 569-572.
23. Chilkoti, A.; Stayton, P. S. J. Am. Chem. Soc. 1995, 117, 10622-10628.
24. Klumb, L. A.; Chu, V.; Stayton, P. S. Biochemistry 1998, 37, 7657-7663.
25. Chilkoti, A.; Boland, T.; Ratner, B. D.; Stayton, P. S. Biophys. J. 1995, 69, 2125-2130.
26. Mrksich, M.; Grunwell, J. R.; Whitesides, G. M. J. Am. Chem. Soc. 1995, 117, 12009-12010.
27. Chilkoti, A.; Tan, P. H.; Stayton, P. S. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 1754-1758.
28. O'Brien, M. J.; Brueck, S. R. J.; Pérez-Luna, V. H.; Tender, L. M.; López, G. P. Biosens. Bioelectron. 1999, 14, 145-154.
29. Raether, H. In Physics of Thin Films; Hass, G., Francombe, M. H., Hoffmann, R. W., Eds.; Academic Press: New York, San Francisco, London, 1977; Vol. 9, 145-261.
30. Bain, C. D.; Whitesides, G. M. J. Am. Chem. Soc. 1989, 111, 7164-7175.
31. Nuzzo, R. G.; Dubois, L. H.; Allara, D. L. J. Am. Chem. Soc. 1990, 112, 558-569.
32. Gupta, V. K.; Abbott, N. L. Science 1997, 276, 1533-1536.
33. Pale-Grosdemande, C; Simon, E. S.; Prime, K. L.; Whitesides, G. M. J. Am. Chem. Soc. 1991, 113, 12-20.
34. The saturation coverage of protein on a surface can be described by random sequential adsorption theory (RSA). According to RSA, this coverage is equivalent to only 55% of the projected protein area. Even after this limit is considered, the numbers indicate a number of biotin groups on the surface an order of magnitude larger than that requited to form a monolayer.
35. Motschmann, H.; Stamm, M.; Toprakcioglu, C. Macromolecules 1991, 24, 3681-3688.
36. Green, N. M. Biochem. J. 1963. 89, 585-591.
37. Zhao, S.; Walker, D. S.; Reichert, W. M. Langmuir 1993, 9, 3166-3173.
38. O'Shannessy, D. J.; Brigham-Burke, M.; Sonesos, K. K.; Hensley, P.; Brooks, I. Anal. Biochem 1993, 212, 457-468.
39. O'Shannessy, D. J.; Winzor, D. J. Anal. Biochem. 1996, 236, 275-283.
40. Schuck, P.; Minton, A. P. Anal. Biochem. 1996, 240, 262-272.
41. Nelson, K. E.; Jung, L. S.; Gamble, L.; Boeckl, M. S.; Naeemi, E.; Campbell, C. T.; Golledge, S. L.; Sasaki, T.; Castner, D. G.; Stayton, P. S., Langmuir, In press.
42. Blankenburg, R.; Meller, P.; Ringsdorf, H.; Salesse, C. Biochemistry 1989, 28, 8214-8221.