The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Kinetics of Metal-Affinity Driven Self-Assembly between Proteins or Peptides and CdSe−ZnS Quantum Dots
Abstract
We present a molecular characterization of metal-affinity driven self-assembly between CdSe−ZnS core−shell quantum dots (QDs) and a series of proteins and peptides appended with various length polyhistidine tags. In particular, we investigated the kinetics of self-assembly between surface-immobilized QDs and proteins/peptides under flow conditions, as well as between freely diffusing QDs and proteins/peptides (solution phase). In the first configuration, QDs were immobilized onto functionalized substrates and then exposed to dye-labeled peptides/proteins. Using evanescent wave excitation, we assessed self-assembly by monitoring the time-dependent changes in the dye fluorescence. In solution, the kinetics of self-assembly was monitored via energy transfer between QDs and dye-labeled proteins/peptides. These measurements allowed determination of the kinetic parameters, including the association and dissociation rates ( k on and k off ) and the apparent binding constant ( K d ). We find that self-assembly is rapid with an equilibrium constant K d -1 ≈ 1 nM for solution self-assembly, confirming that metal-affinity interactions provide QD bioconjugates that are functional and stable.
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Cites
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Metadata
- Authors
- Sapsford, K. E., Pons, T., Medintz, I. L., Higashiya, S., Brunel, F. M., Dawson, P. E., & Mattoussi, H.
- Venue
- The Journal of Physical Chemistry C
- Publisher
- American Chemical Society (ACS)
- Published
- 2007-07-19
- Volume
- 111
- Issue
- 31
- Pages
- 11528-11538
- ISSN
- 1932-7447 (ISSN-L)
- 1932-7455
- OpenAlex
- W2041630712
- Cited by
- 276
- References
- 35
- FWCI
- 9.51
- Type
- journal article
- Language
- en
- Open access
- closed
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