Hostname: page-component-586b7cd67f-vdxz6 Total loading time: 0 Render date: 2024-11-29T09:43:29.678Z Has data issue: false hasContentIssue false

Quantum Dots as Inorganic DNA-Binding Proteins

Published online by Cambridge University Press:  15 February 2011

Catherine J. Murphy
Affiliation:
Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208 [email protected]
Eric B. Brauns
Affiliation:
Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208 [email protected]
Latha Gearheart
Affiliation:
Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208 [email protected]
Get access

Abstract

Semiconductor quantum dots of cadmium sulfide, CdS, are approximately the size of proteins and are photoluminescent in the red, yellow, or green, depending on surface preparation. This photoluminescence is very sensitive to the Nature and amount of adsorbates. We have found that DNAs with intrinsic curvature adsorb more strongly to the surface of 47 Å CdS quantum dots, as judged by concentration-dependent changes in photoluminescence. The binding constants we obtain are similar to those found for nonspecific protein-DNA interactions. The surface groups of the CdS substrate also influence DNA adsorption. Thus these protein-sized colloidal particles can be used in chemical sensing applications for curved or kinked DNA; DNA with unusual structures is thought to influence biological function such as transcription.

Type
Research Article
Copyright
Copyright © Materials Research Society 1997

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

1. For example, see (a) Gartenberg, M.R. and Crothers, D.M., J. Mol. Biol. 219, p. 217;Google Scholar
(b) Perez-Martin, J. and Espinosa, M., J. Mol. Biol. 241, p. 7 (1994).Google Scholar
2. (a)Mahtab, R., Rogers, J.P., J.P., , and Murphy, C.J., J. Am. Chem. Soc. 117, p. 9099 (1995).Google Scholar
(b) Mahtab, R., Rogers, J.P., Singleton, C.P., and Murphy, C.J., J. Am. Chem. Soc. 118, p. 7028 (1996).Google Scholar
3. (a)Spolar, R.S. and Record, M.T. Jr., Science 263, p. 777 (1994);Google Scholar
(b) Ramsden, J.J. and Dreier, J., Biochemistry 35, p. 3746 (1996).Google Scholar
4.Shrader, T.E. and Crothers, D.M., Proc. Natl. Acad. Sci. USA 86, p. 7418 (1989).Google Scholar
5.Nosaka, Y., Ohata, N., Fukuyama, T., and Fuji, N., J. Colloid Interface Science. 155, p. 23 (1993).Google Scholar
6.Brus, L.E., J. Chem. Phys. 80, p. 4403 (1984).Google Scholar
7.Bigham, S.R. and Coffer, J.L., J. Phys. Chem. 96, p. 10581 (1992).Google Scholar
8.Simha, R., Frisch, H.L., and Eirich, F.R., J. Phys. Chem. 57, p. 584 (1953).Google Scholar
9.Winter, R.B., Berg, O.G., and von Hippel, P.H., Biochemistry 20, p. 6961 (1981).Google Scholar
10.Spanhel, L., Haase, M., Weiler, H., and Henglein, A., J. Am. Chem. Soc. 109, p. 5649 (1987).Google Scholar