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Combinatorial Approaches to Peptide-Encapsulated CdS Nanoclusters

Published online by Cambridge University Press:  10 February 2011

G. Spreitzer
Affiliation:
Duquesne University, Department of Chemistry and Biochemistry, 308 Mellon Hall, Pittsburgh, PA 15282, [email protected]
J. M. Whitling
Affiliation:
Duquesne University, Department of Chemistry and Biochemistry, 308 Mellon Hall, Pittsburgh, PA 15282, [email protected]
D. W. Wright
Affiliation:
Duquesne University, Department of Chemistry and Biochemistry, 308 Mellon Hall, Pittsburgh, PA 15282, [email protected]
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Abstract

As many properties of group II-VI semiconductor nanocrystallites arise from their quantum confined nature, the synthesis of these clusters is of great interest. The challenge of synthesizing functional nanoclusters is, however, complicated by the limited stability of metalchalcogen surfaces under highly oxidizing conditions and Ostwald ripening. Our objectives are to develop methods for the synthesis of biogenic CdS semiconductor nanocrystallites that address the following issues: (1) What properties of the ligand peptide are important in stabilizing and producing CdS particles of any desired size? (2) Will hybrid peptides using nonnatural amino acids stabilize the nanoclusters while incorporating new surface functionality? (3) Is it possible to use novel peptides to modify the particle surface, thereby, controlling the photophysical properties of the CdS cluster? Our approach consists of parallel combinatorial techniques and computational methods for the discovery and optimization of peptide and peptidomimetic ligands to stabilize size-defined clusters of CdS. The effects of cysteine separation on CdS particle size by varying the number of bonds with rotational freedom within the spacer amino acids is examined. Furthermore, the properties of the resulting CdS nanoclusters are reported.

Type
Research Article
Copyright
Copyright © Materials Research Society 2000

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References

1.. (a) Gratzel, M., Acc. Chem. Res. 14, p. 376 (1981).Google Scholar
(b) Capasso, F., Science 235, p. 172 (1987).Google Scholar
(c) Henglein, A., Chem. Rev. 89, p. 1861 (1989).Google Scholar
(d) Weller, H., Angew. Chem. Int. Ed. Engl. 32, p. 41 (1993).Google Scholar
(e) Stucky, G., MacDougall, J., Science 247, p. 664 (1990).Google Scholar
(f) Murray, C.B., Norris, D.J., Bawendi, M.G., J. Am. Chem. Soc. 115, p. 8706 (1993).Google Scholar
(g) Murphy, C.J., J. Cluster Sci. 7, p. 341 (1996).Google Scholar
2. Reese, R. N., Winge, D. R., J. Biol. Chem. 263, p. 12832 (1988);Google Scholar
Reese, R. N., White, C. A., Winge, D.R., Plant Physiol. 98, p. 225 (1992);Google Scholar
Dameron, C.T., Smith, B.R., Winge, D.R., Biol, J.. Chem. 264, p. 17355 (1989);Google Scholar
Dameron, C.T., Winge, D.R., Inorg. Chem. 29, p. 1343 (1990);Google Scholar
Winge, D.R., Cameron, C.T., Mehra, R.K., in Metallothioneins: Synthesis, Structure, and Properties of Metallothioneins, Phytochelatins, and Metal Complexes, edited by Stilman, M.J., Shaw, C.F., Suzuki, K.T. (VCH Publishers, New York, 1992) p. 257;Google Scholar
Dameron, C.T., Reese, R.N., Mehra, R.K., Kortan, A.R., Carroll, P.J., Steigerwald, M.L., Brus, L.E., Winge, D.R., Science 338, p. 596 (1989).Google Scholar
3. Grill, E., Winnacker, E.-L., Zenk, M.H., Science 230, p. 674 (1985); Rauser, W.E., Annu. Rev. Biochem. 59, p. 61 (1990). The number of dipeptide (γ-GluCys) repeats in phytochelatins typically ranges from 2 to 13. The number of dipeptide repeats commonly observed in the capping of CdS nanoclusters is 2 to 4.Google Scholar
4. Dameron, C.T., Winge, D.R., Trends Biotechnol. 8, p. 3 (1990); Bae, W., Mehra, R. K., J. Inorg. Biochem. 68, p. 201 (1997).Google Scholar
5. The Cα-Cα, distance is based on an extended conformation. These values represent the maximum distance separating the cysteine residues and are a reasonable first approximation for the S-S distances of the chelate peptide.Google Scholar
6. The Chiron Mimetope and PepSets technology (Chiron Technologies, San Diego, CA) has recently been reviewed by Pirrung, M.C., Chem. Rev. 9, p. 473 (1997).Google Scholar
7. Nguyen, L., Kho, R., Bae, W., Mehra, R. K., Chemosphere 38, p. 155 (1999).Google Scholar
8. Bae, W., Mehra, R.K., J. Inorg. Biochem. 69, p. 33 (1998).Google Scholar
9. Fisher, C.H., Weller, H., Katsikas, L., Henglein, A., Langmuir 5, p. 429 (1989); H. Determann, Gelchromatographie (Springer, Berlin 1967) p. 115.Google Scholar
10. Brus, L.E., J. Chem. Phys. 79, p. 5566 (1983); L.E. Brus, J. Chem. Phys. 80, p. 4403 (1984); Rossetti, R., Ellison, J.L., Gibson, J.M., Brus, L.E. J. Chem. Phys. 80, p. 4464 (1984).Google Scholar
11. Dameron, C.T., Dance, I.G., Biomimetic Materials Chemistry, edited by Mann, S. (VCH Publishers, New York, 1996) p. 69.05990209 Google Scholar