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Probing Bioluminescence Resonance Energy Transfer in Quantum Rod–Luciferase Nanoconjugates

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Department of Chemistry, Syracuse University, Syracuse, New York 13244, United States
Syracuse Biomaterials Institute, Syracuse University, Syracuse, New York 13244, United States
§ Department of Chemistry, Connecticut College, New London, Connecticut 06320, United States
Cite this: ACS Nano 2016, 10, 2, 1969–1977
Publication Date (Web):January 13, 2016
https://doi.org/10.1021/acsnano.5b05966
Copyright © 2016 American Chemical Society

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    Abstract

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    We describe the necessary design criteria to create highly efficient energy transfer conjugates containing luciferase enzymes derived from Photinus pyralis (Ppy) and semiconductor quantum rods (QRs) with rod-in-rod (r/r) microstructure. By fine-tuning the synthetic conditions, CdSe/CdS r/r-QRs were prepared with two different emission colors and three different aspect ratios (l/w) each. These were hybridized with blue, green, and red emitting Ppy, leading to a number of new BRET nanoconjugates. Measurements of the emission BRET ratio (BR) indicate that the resulting energy transfer is highly dependent on QR energy accepting properties, which include absorption, quantum yield, and optical anisotropy, as well as its morphological and topological properties, such as aspect ratio and defect concentration. The highest BR was found using r/r-QRs with lower l/w that were conjugated with red Ppy, which may be activating one of the anisotropic CdSe core energy levels. The role QR surface defects play on Ppy binding, and energy transfer was studied by growth of gold nanoparticles at the defects, which indicated that each QR set has different sites. The Ppy binding at those sites is suggested by the observed BRET red-shift as a function of Ppy-to-QR loading (L), where the lowest L results in highest efficiency and furthest shift.

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    The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acsnano.5b05966.

    • Details of quantum rod synthesis, protein expression, conjugate assembly, and measurements. Tables S1–S3, Figures S1–S8 (PDF)

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