Site-specific protein immobilization by Staudinger ligation

Journal of the American Chemical Society

Volumn 125, Issue 39, 2003, Pages 11790-11791

  Soellner, Matthew B ^a   Dickson, Kimberly A ^a   Nilsson, Bradley L ^a   Raines, Ronald T ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN ANTIBODY COMPLEX; ARTICLE; COVALENT BOND; DERIVATIZATION; ENZYME ACTIVITY; ENZYME SPECIFICITY; PROTEIN IMMOBILIZATION; PROTEIN PROTEIN INTERACTION; REACTION ANALYSIS; RNA CLEAVAGE; STAUDINGER REACTION;

AMINO ACID SEQUENCE; AZIDES; COMBINATORIAL CHEMISTRY TECHNIQUES; ENZYMES, IMMOBILIZED; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; POLYETHYLENE GLYCOLS; RIBONUCLEASES;

EID: 0141843623     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja036712h     Document Type: Article

References (28)

1. For reviews, see: (a) Kodadek, T. Chem. Biol. 2001, 8, 105-115.
2. (b) Zhu, H.; Snyder, M. Curr. Opin. Chem. Biol. 2001, 5, 40-45.
3. (c) Lee, Y.-S.; Mrksich, M. Trends Biotechnol. 2002, 20, S14-S18.
4. (a) Houseman, B. T.; Huh, J. H.; Kron, S. J.; Mrksich, M. Nat. Biotechnol. 2002, 20, 270-274.
5. (b) Lesaicherre, M.-L.; Uttamchandani, M.; Chen, G. Y. J.; Yao, S. Q. Bioorg. Med. Chem. Lett. 2002, 12, 2079-2083.
6. (c) Toepert, F.; Knaute, T.; Guffler, S.; Pirés, J. R.; Matzdorf, T.; Oschkinat, H.; Schneider-Mergener, J. Angew. Chem., Int. Ed. 2003, 42, 1136-1140.
7. MacBeath, G.; Schreiber, S. L. Science 2000, 289, 1760-1763.
8. Zhu, H.; Bilgin, M.; Bangham, R.; Hall, D.; Casamayor, A.; Bertone, P.; Lan, N.; Jansen, R.; Bidlingmaier, S.; Houfek, T.; Mitchell, T.; Miller, P.; Dean, R. A.; Gerstein, M.; Snyder, M. Science 2001, 293, 2101-2105.
9. Peluso, P.; Wilson, D. S.; Do, D.; Tran, H.; Venkatasubbaiah, M.; Quincy, D.; Heidecker, B.; Poindexter, K.; Tolani, H.; Phelan, M.; Witte, K.; Jung, L. S.; Wanger, P.; Nock, S. Anal. Biochem. 2003, 312, 113-124.
10. For leading references, see: (a) Soellner, M. B.; Nilsson, B. L.; Raines, R. T. J. Org. Chem. 2002, 67, 4993-4996.
11. (b) Nilsson, B. L.; Hondal, R. J.; Soellner, M. B.; Raines, R. T. J. Am. Chem. Soc. 2003, 125, 5268-5269.
12. (a) Richards, F. M. Compt. Rend. Lab. Carlsberg, Ser. Chim. 1955, 29, 329-346.
13. (b) Richards, F. M.; Vithayathil, P. J. J. Biol. Chem. 1959, 234, 1459-1465.
14. For a review, see: (c) Raines, R. T. Chem. Rev. 1998, 98, 1045-1065.
15. (a) Potts, J. T., Jr.; Young, D. M.; Anfinsen, C. B. J. Biol. Chem. 1963, 238, 2593-2594.
16. (b) Connelly, P. R.; Varadarajan, R.; Sturtevant, J.; Richards, F. M. Biochemistry 1990, 29; 6108-6114.
17. r ≈ 3400) prevented the nonspecific attachment of protein to the glass surface.
18. r 2284.4).
19. 2-6-tetramethylrhodamine (6 μM) was added to each spot. At various times, an aliquot was removed from the slide, and its fluorescence was determined.
20. Immunoassays were performed on each spot by adding rabbit anti-RNase A IgG (2 μg/mL) for 30 min. The slide was then washed with PBS. Each spot was incubated with an Alexa Fluor 488-conjugated secondary antibody (1 μg/mL) for 30 min. The slide was then washed with PBS, and its fluorescence was determined.
21. 2.
22. 2.
23. -8 M; ref 7b) could dissociate to some extent during the timecourse of assays.
24. Gregory, M. J.; Bruice, T. C. J. Am. Chem. Soc. 1967, 89, 2121-2126.
25. 2.
26. The side-chain amino groups of Lys7, Lys41, and Lys66 are known to be important for catalysis (ref 7c).
27. For a biosynthetic route, see: (a) Kiick, K. L.; Saxon, E.; Tirrell, D. A.; Bertozzi, C. R. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 19-24.
28. For the basis of a semisynthetic route, see: (b) Muir, T. W. Annu. Rev. Biochem. 2003, 72, 249-289.