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Förster Resonance Energy Transfer between Core/Shell Quantum Dots and Bacteriorhodopsin.

Griep MH, Winder EM, Lueking DR, Garrett GA, Karna SP, Friedrich CR - Mol Biol Int (2012)

Bottom Line: An energy transfer relationship between core-shell CdSe/ZnS quantum dots (QDs) and the optical protein bacteriorhodopsin (bR) is shown, demonstrating a distance-dependent energy transfer with 88.2% and 51.1% of the QD energy being transferred to the bR monomer at separation distances of 3.5 nm and 8.5 nm, respectively.Fluorescence lifetime measurements isolate nonradiative energy transfer, other than optical absorptive mechanisms, with the effective QD excited state lifetime reducing from 18.0 ns to 13.3 ns with bR integration, demonstrating the Förster resonance energy transfer contributes to 26.1% of the transferred QD energy at the 3.5 nm separation distance.The established direct energy transfer mechanism holds the potential to enhance the bR spectral range and sensitivity of energies that the protein can utilize, increasing its subsequent photocurrent generation, a significant potential expansion of the applicability of bR in solar cell, biosensing, biocomputing, optoelectronic, and imaging technologies.

View Article: PubMed Central - PubMed

Affiliation: Department of Mechanical Engineering Mechanics, Michigan Technological University, 815 RL Smith, 1400 Townsend Drive, Houghton, MI 49931, USA.

ABSTRACT
An energy transfer relationship between core-shell CdSe/ZnS quantum dots (QDs) and the optical protein bacteriorhodopsin (bR) is shown, demonstrating a distance-dependent energy transfer with 88.2% and 51.1% of the QD energy being transferred to the bR monomer at separation distances of 3.5 nm and 8.5 nm, respectively. Fluorescence lifetime measurements isolate nonradiative energy transfer, other than optical absorptive mechanisms, with the effective QD excited state lifetime reducing from 18.0 ns to 13.3 ns with bR integration, demonstrating the Förster resonance energy transfer contributes to 26.1% of the transferred QD energy at the 3.5 nm separation distance. The established direct energy transfer mechanism holds the potential to enhance the bR spectral range and sensitivity of energies that the protein can utilize, increasing its subsequent photocurrent generation, a significant potential expansion of the applicability of bR in solar cell, biosensing, biocomputing, optoelectronic, and imaging technologies.

No MeSH data available.


Related in: MedlinePlus

QD quenching effects of bR (PM patch and bR monomer forms) when linked to a CdSe/ZnS QD via (a) EDC and (b) biotin/streptavidin binding scheme. Inset images illustrate each linkage and estimate the QD-bR retinal separation distance to be 3.5 nm and 8.5 nm for the EDC and biotin/streptavidin linkages, respectively.
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fig3: QD quenching effects of bR (PM patch and bR monomer forms) when linked to a CdSe/ZnS QD via (a) EDC and (b) biotin/streptavidin binding scheme. Inset images illustrate each linkage and estimate the QD-bR retinal separation distance to be 3.5 nm and 8.5 nm for the EDC and biotin/streptavidin linkages, respectively.

Mentions: This study utilizes both short (EDC) and long (biotin/streptavidin) linking schemes to ensure QD-bR nanoscale proximity. At these varied separation distances, the energy coupling relationship between QDs and bR, in both the purple membrane fragment and bR monomer form, was analyzed. The QD quenching effects of each bR form at the given separation distance is shown in Figure 3.


Förster Resonance Energy Transfer between Core/Shell Quantum Dots and Bacteriorhodopsin.

Griep MH, Winder EM, Lueking DR, Garrett GA, Karna SP, Friedrich CR - Mol Biol Int (2012)

QD quenching effects of bR (PM patch and bR monomer forms) when linked to a CdSe/ZnS QD via (a) EDC and (b) biotin/streptavidin binding scheme. Inset images illustrate each linkage and estimate the QD-bR retinal separation distance to be 3.5 nm and 8.5 nm for the EDC and biotin/streptavidin linkages, respectively.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3376779&req=5

fig3: QD quenching effects of bR (PM patch and bR monomer forms) when linked to a CdSe/ZnS QD via (a) EDC and (b) biotin/streptavidin binding scheme. Inset images illustrate each linkage and estimate the QD-bR retinal separation distance to be 3.5 nm and 8.5 nm for the EDC and biotin/streptavidin linkages, respectively.
Mentions: This study utilizes both short (EDC) and long (biotin/streptavidin) linking schemes to ensure QD-bR nanoscale proximity. At these varied separation distances, the energy coupling relationship between QDs and bR, in both the purple membrane fragment and bR monomer form, was analyzed. The QD quenching effects of each bR form at the given separation distance is shown in Figure 3.

Bottom Line: An energy transfer relationship between core-shell CdSe/ZnS quantum dots (QDs) and the optical protein bacteriorhodopsin (bR) is shown, demonstrating a distance-dependent energy transfer with 88.2% and 51.1% of the QD energy being transferred to the bR monomer at separation distances of 3.5 nm and 8.5 nm, respectively.Fluorescence lifetime measurements isolate nonradiative energy transfer, other than optical absorptive mechanisms, with the effective QD excited state lifetime reducing from 18.0 ns to 13.3 ns with bR integration, demonstrating the Förster resonance energy transfer contributes to 26.1% of the transferred QD energy at the 3.5 nm separation distance.The established direct energy transfer mechanism holds the potential to enhance the bR spectral range and sensitivity of energies that the protein can utilize, increasing its subsequent photocurrent generation, a significant potential expansion of the applicability of bR in solar cell, biosensing, biocomputing, optoelectronic, and imaging technologies.

View Article: PubMed Central - PubMed

Affiliation: Department of Mechanical Engineering Mechanics, Michigan Technological University, 815 RL Smith, 1400 Townsend Drive, Houghton, MI 49931, USA.

ABSTRACT
An energy transfer relationship between core-shell CdSe/ZnS quantum dots (QDs) and the optical protein bacteriorhodopsin (bR) is shown, demonstrating a distance-dependent energy transfer with 88.2% and 51.1% of the QD energy being transferred to the bR monomer at separation distances of 3.5 nm and 8.5 nm, respectively. Fluorescence lifetime measurements isolate nonradiative energy transfer, other than optical absorptive mechanisms, with the effective QD excited state lifetime reducing from 18.0 ns to 13.3 ns with bR integration, demonstrating the Förster resonance energy transfer contributes to 26.1% of the transferred QD energy at the 3.5 nm separation distance. The established direct energy transfer mechanism holds the potential to enhance the bR spectral range and sensitivity of energies that the protein can utilize, increasing its subsequent photocurrent generation, a significant potential expansion of the applicability of bR in solar cell, biosensing, biocomputing, optoelectronic, and imaging technologies.

No MeSH data available.


Related in: MedlinePlus