Abstract
Resonance energy transfer in self-assembled hybrid structures formed by water-soluble semiconductor CdSe/ZnS quantum dots (QD) with a cysteine shell and the Exiguobacterium sibiricum retinal protein (ESR) in three modifications, with and without a 6-membered C-terminal histidine tag, and with both the histidine tag and C-terminal cysteine residue. Steady-state and time-resolved fluorescence spectroscopy was used to demonstrate that nonradiative energy transfer from QD onto the ESR protein depends on the strength of intermolecular interactions in the hybrid complex. A shift from electrostatic interactions in the QD-ESR donor-acceptor pair to coordinate bond with an additional disulfide bond resulted in an increase of the energy transfer efficiency from 40 to over 90%. The proposed method to produce noncovalent conjugates from QDs and light-sensitive proteins can be a promising one for biomedical applications, as well as for the development of new solar energy accumulation systems.
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Abbreviations
- ESR:
-
Exiguobacterium sibiricum retinal protein
- QD:
-
quantum dots
- QD510:
-
QD with photoluminescence band maximum at 510 nm
- RC:
-
reaction center
- BR:
-
Halobacterium salinarum bacteriorhodopsin
- PM:
-
purple membranes
- DDM:
-
n-dodecyl-β-D-maltoside
- FRET:
-
Förster resonance energy transfer
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Original Russian Text © E.P. Lukashev, L.E. Petrovskaya, M.V. Tretyak, E.A. Kryukova, S.V. Sizova, V.A. Oleinikov, 2018, published in Bioorganicheskaya Khimiya, 2018, Vol. 44, No. 6, pp. 655–663.
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Lukashev, E.P., Petrovskaya, L.E., Tretyak, M.V. et al. Formation of an Efficient Energy Transfer Complex between Quantum Dots and Exiguobacterium sibiricum Retinal Protein via the Histidine-Cysteine Anchor. Russ J Bioorg Chem 44, 687–694 (2018). https://doi.org/10.1134/S1068162018050114
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DOI: https://doi.org/10.1134/S1068162018050114