A Self-Assembled Monolayer for the Binding and Study of Histidine-Tagged Proteins by Surface Plasmon Resonance

Analytical Chemistry - Tập 68 Số 3 - Trang 490-497 - 1996
George B. Sigal1, Cynthia Bamdad1, Alcide Barberis1, Jack L. Strominger1, George M. Whitesides1
1Departments of Chemistry and Biochemistry and the Committee for Higher Degrees in Biophysics, Harvard University, Cambridge, Massachusetts 02138

Tóm tắt

Từ khóa


Tài liệu tham khảo

Liedberg B., 1983, Sens. Actuators, 4, 304, 10.1016/0250-6874(83)85036-7

Daniels P. B., 1988, Sens. Actuators, 16, 18

Löfås S., 1990, Chem. Commun., 1526, 1528

Raether H., 1977, Phys. Thin Films, 9, 261

Stenberg E., 1991, J. Colloid Interface Sci., 143, 526, 10.1016/0021-9797(91)90284-F

Flanagan M. T., 1984, Electron. Lett., 20, 970, 10.1049/el:19840660

Davies J., 1994, Langmuir, 10, 2661

Dubois L. H., 1992, Annu. Rev. Phys. Chem., 43, 463, 10.1146/annurev.pc.43.100192.002253

Whitesides, G. M.; Gorman, C. G. InHandbook of Surface Imaging and Visualization; Hubbard, A. T., Ed.; CRC Press:  Boca Raton, FL, 1995; pp 713−733.

Spinke J., 1993, Langmuir, 9, 1825, 10.1021/la00031a033

Hochuli E., 1987, J. Chromatogr., 411, 184

Gentz R., 1989, Proc. Natl. Acad. Sci. U.S.A., 86, 824, 10.1073/pnas.86.3.821

Chung S., 1995, Proc. Natl. Acad. Sci. U.S.A., 91, 12658

Barberis A., 1995, Cell, 81, 368, 10.1016/0092-8674(95)90389-5

McCrackin F. L., 1963, J. Res. Natl. Bur. Stand., Sect. A, 67, 377

Overman L. E., 1974, Synthesis, 59, 60

Prime K. L., 1993, J. Am. Chem. Soc., 115, 10721, 10.1021/ja00076a032

Pale-Grosdemange C., 1991, J. Am. Chem. Soc., 113, 20, 10.1021/ja00001a002

Laibinis P. E., 1992, J. Phys. Chem., 96, 5105, 10.1021/j100191a065

Corrections, 1976, J. Electron Spectrosc., 8, 137

Since, 1994, J. Phys. Chem., 98, 7646

Zhao Y., 1991, Eur. J. Biochem., 202, 1119, 10.1111/j.1432-1033.1991.tb16478.x

The, 1977, R. M. A.

Koleske A. J., 1994, Nature, 368, 469, 10.1038/368466a0

The Ni−NTA surface we describe here has already been applied in probing the interactions between an array of defined proteins and protein fragments involved in gene regulation in yeast (ref 14). Without exception, a strong correlation was found between the strengths of the interactions observed in vitro and the known biological activity of the molecules. These data indicate that, at least within the range of the interaction strengths tested (10-6−10-7M), the surface can be used to quantitate certain protein−protein interactions accurately. More experience with the method is, however, required to evaluate its generality.

Schlatter D., 1993, Biosens. Bioelectron., 8, 116, 10.1016/0956-5663(93)80059-X

Dahint R., 1994, Anal. Chem., 66, 2892, 10.1021/ac00090a015

Steibel, 1994, Biosens. Bioelectron., 9, 146

Janata J., 1988, Anal. Chem., 60, 74, 10.1021/ac00163a004

Gudibande S. R., 1992, J. Mol. Cell. Probes, 6, 503

Gershon P. D., 1995, J. Immunol. Methods, 183, 76, 10.1016/0022-1759(95)00032-6