Abstract
Using a combination of two amino acids, histidine and N-acetyl-cysteine, to replace the original organic capping groups of (CdSe)ZnS quantum dots, water-soluble and highly luminescent (CdSe)ZnS quantum dots have been successfully prepared at pH 8. Characterization by steady-state and time-resolved photoluminescence spectroscopy, and transient absorption spectroscopy, demonstrate that the electronic properties of these quantum dots exceed those of the original as-synthesized samples dissolved in a more-conventional organic solvent. Furthermore, these amino acid-stabilized quantum dots have been assembled onto a cellulose substrate via cellulose binding proteins that specifically bind to cellulose and was genetically engineered to harbor dual hexahistidine tags at the N- and C-termini to confer binding with the zinc(ii) on the quantum dot surface. The spectroscopic measurements show that the protein-bound quantum dots continue to retain their desirable electronic properties when bound on the substrate. Meanwhile, the specific and very selective binding properties of the proteins have remained effective.
| Original language | English |
|---|---|
| Pages (from-to) | 1027-1033 |
| Number of pages | 7 |
| Journal | Photochemical and Photobiological Sciences |
| Volume | 6 |
| Issue number | 9 |
| DOIs | |
| Publication status | Published - 2007 |
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ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Cell Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biophysics
Cite this
Photophysics of (CdSe)ZnS colloidal quantum dots in an aqueous environment stabilized with amino acids and genetically-modified proteins. / Ai, Xin; Xu, Qi; Jones, Marcus; Song, Qing; Ding, Shi You; Ellingson, Randy J.; Himmel, Mike; Rumbles, Gary.
In: Photochemical and Photobiological Sciences, Vol. 6, No. 9, 2007, p. 1027-1033.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Photophysics of (CdSe)ZnS colloidal quantum dots in an aqueous environment stabilized with amino acids and genetically-modified proteins
AU - Ai, Xin
AU - Xu, Qi
AU - Jones, Marcus
AU - Song, Qing
AU - Ding, Shi You
AU - Ellingson, Randy J.
AU - Himmel, Mike
AU - Rumbles, Gary
PY - 2007
Y1 - 2007
N2 - Using a combination of two amino acids, histidine and N-acetyl-cysteine, to replace the original organic capping groups of (CdSe)ZnS quantum dots, water-soluble and highly luminescent (CdSe)ZnS quantum dots have been successfully prepared at pH 8. Characterization by steady-state and time-resolved photoluminescence spectroscopy, and transient absorption spectroscopy, demonstrate that the electronic properties of these quantum dots exceed those of the original as-synthesized samples dissolved in a more-conventional organic solvent. Furthermore, these amino acid-stabilized quantum dots have been assembled onto a cellulose substrate via cellulose binding proteins that specifically bind to cellulose and was genetically engineered to harbor dual hexahistidine tags at the N- and C-termini to confer binding with the zinc(ii) on the quantum dot surface. The spectroscopic measurements show that the protein-bound quantum dots continue to retain their desirable electronic properties when bound on the substrate. Meanwhile, the specific and very selective binding properties of the proteins have remained effective.
AB - Using a combination of two amino acids, histidine and N-acetyl-cysteine, to replace the original organic capping groups of (CdSe)ZnS quantum dots, water-soluble and highly luminescent (CdSe)ZnS quantum dots have been successfully prepared at pH 8. Characterization by steady-state and time-resolved photoluminescence spectroscopy, and transient absorption spectroscopy, demonstrate that the electronic properties of these quantum dots exceed those of the original as-synthesized samples dissolved in a more-conventional organic solvent. Furthermore, these amino acid-stabilized quantum dots have been assembled onto a cellulose substrate via cellulose binding proteins that specifically bind to cellulose and was genetically engineered to harbor dual hexahistidine tags at the N- and C-termini to confer binding with the zinc(ii) on the quantum dot surface. The spectroscopic measurements show that the protein-bound quantum dots continue to retain their desirable electronic properties when bound on the substrate. Meanwhile, the specific and very selective binding properties of the proteins have remained effective.
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U2 - 10.1039/b706471c
DO - 10.1039/b706471c
M3 - Article
C2 - 17721603
AN - SCOPUS:34548160164
VL - 6
SP - 1027
EP - 1033
JO - Photochemical and Photobiological Sciences
JF - Photochemical and Photobiological Sciences
SN - 1474-905X
IS - 9
ER -