全部 标题 作者
关键词 摘要

OALib Journal期刊
ISSN: 2333-9721
费用:99美元

查看量下载量

相关文章

更多...

F?rster Resonance Energy Transfer between Core/Shell Quantum Dots and Bacteriorhodopsin

DOI: 10.1155/2012/910707

Full-Text   Cite this paper   Add to My Lib

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 F?rster 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. 1. Introduction Integrated nano biosystems are expected to offer applications in multiple technologies, such as biodetection and sensing [1, 2], biomedical diagnostics [3], single molecule dynamics [4], and photovoltaics [5]. In this work, the fundamental properties of such multifunctional hybrid nano biosystems involving core-shell quantum dots (QDs) and the optical protein bacteriorhodopsin (bR) are presented. Bacteriorhodopsin has been a subject of intense study over the past four decades due to its photoconducting properties and exceptionally high long-term stability against thermal, chemical, and photochemical degradation [6–8]. As a retinal protein found in the cell membrane of the extremophile Halobacterium salinarum, it is utilized to generate a proton motive force that energizes ATP synthase to drive the conversion of ADP and Pi to ATP and H2O, thereby providing the energy to drive the cell’s internal machinery [9]. The proton motive force is achieved when bR’s attached retinal chromophore absorbs photons in the 570?nm region, resulting in a cis-trans isomerization of the retinal. This structural alteration initiates proton transport from the retinal region to the extracellular side of the membrane creating a proton gradient within the membrane, with subsequent reprotonation from the cytoplasm [10]. This proton gradient across the cell membrane, which facilitates ATP synthesis in living systems, can be utilized to produce a measurable electrical response in engineered applications. Applications of bR require it to be extracted from the

References

[1]  P. Alivisatos, “The use of nanocrystals in biological detection,” Nature Biotechnology, vol. 22, no. 1, pp. 47–52, 2004.
[2]  R. Elghanian, J. J. Storhoff, R. C. Mucic, R. L. Letsinger, and C. A. Mirkin, “Selective colorimetric detection of polynucleotides based on the distance-dependent optical properties of gold nanoparticles,” Science, vol. 277, no. 5329, pp. 1078–1081, 1997.
[3]  D. Gei?ler, L. J. Charbonnière, R. F. Ziessel, N. G. Butlin, H. G. L?hmannsr?ben, and N. Hildebrandt, “Quantum dot biosensors for ultrasensitive multiplexed diagnostic,” Angewandte Chemies, vol. 49, no. 8, pp. 1396–1401, 2010.
[4]  S. Weiss, “Fluorescence spectroscopy of single biomolecules,” Science, vol. 283, no. 5408, pp. 1676–1683, 1999.
[5]  T. Hasobe, S. Fukuzumi, and P. V. Kamat, “Ordered assembly of protonated porphyrin driven by single-wall carbon nanotubes. J- And H-aggregates to nanorods,” Journal of the American Chemical Society, vol. 127, no. 34, pp. 11884–11885, 2005.
[6]  W. W. Wang, G. K. Knopf, and A. S. Bassi, “Photoelectric properties of a detector based on dried bacteriorhodopsin film,” Biosensors and Bioelectronics, vol. 21, no. 7, pp. 1309–1319, 2006.
[7]  J.-A. He, L. Samuelson, L. Li, J. Kumar, and S. K. Tripathy, “Bacteriorhodopsin thin film assemblies—immobilization, properties, and applications,” Advanced Materials, vol. 11, no. 6, pp. 435–446, 1999.
[8]  D. Oesterhelt and W. Stoeckenius, “Rhodopsin-like protein from the purple membrane of Halobacterium halobium,” Nature, vol. 233, no. 39, pp. 149–152, 1971.
[9]  U. Haupts, J. Tittor, and D. Oesterhelt, “Closing in on bacteriorhodopsin: progress in understanding the molecule,” Annual Review of Biophysics and Biomolecular Structure, vol. 28, pp. 367–399, 1999.
[10]  S. B. Hwang and W. Stoeckenius, “Purple membrane vesicles: morphology and proton translocation,” Journal of Membrane Biology, vol. 33, no. 3-4, pp. 325–350, 1977.
[11]  N. A. Hampp, “Bacteriorhodopsin: mutating a biomaterial into an optoelectronic material,” Applied Microbiology and Biotechnology, vol. 53, no. 6, pp. 633–639, 2000.
[12]  T. Miyasaka, K. Koyama, and I. Itoh, “Quantum conversion and image detection by a bacteriorhodopsin-based artificial photoreceptor,” Science, vol. 255, no. 5042, pp. 342–344, 1992.
[13]  J. Wang, S.-K. Yoo, L. Song, and M. A. El-Sayed, “Molecular mechanism of the differential photoelectric response of bacteriorhodopsin,” Journal of Physical Chemistry B, vol. 101, no. 17, pp. 3420–3423, 1997.
[14]  P. Bertoncello, D. Nicolini, C. Paternolli, V. Bavastrello, and C. Nicolini, “Bacteriorhodopsin-based Langmuir-Schaefer films for solar energy capture,” IEEE Transactions on Nanobioscience, vol. 2, no. 2, pp. 124–132, 2003.
[15]  V. Thavasi, T. Lazarova, S. Filipek et al., “Study on the feasibility of bacteriorhodopsin as bio-photosensitizer in excitonic solar cell: a first report,” Journal of Nanoscience and Nanotechnology, vol. 9, no. 3, pp. 1679–1687, 2009.
[16]  R. Koch, A. S. Lipton, S. Filipek, and V. Renugopalakrishnan, “Arginine interactions with anatase TiO2 (100) surface and the perturbation of 49Ti NMR chemical shifts—a DFT investigation: relevance to Renu-Seeram bio solar cell,” Journal of Molecular Modeling, vol. 17, no. 6, pp. 1467–1472, 2011.
[17]  R. Renugopalakrishnan, K. Khizroev, A. Anand, P. Pingzuo, and L. Lindvold, “Future memory storage technology: protein-based memory devices may facilitate surpassing Moore's law,” IEEE Transactions on Magnetics, vol. 43, no. 2, pp. 773–775, 2007.
[18]  T. M. Jovin, “Quantum dots finally come of age,” Nature Biotechnology, vol. 21, no. 1, pp. 32–33, 2003.
[19]  D. Gerion, F. Pinaud, S. C. Williams et al., “Synthesis and properties of biocompatible water-soluble silica-coated CdSe/ZnS semiconductor quantum dots,” Journal of Physical Chemistry B, vol. 105, no. 37, pp. 8861–8871, 2001.
[20]  T. F?rster, “10th spiers memorial lecture. Transfer mechanisms of electronic excitation,” Discussions of the Faraday Society, vol. 27, pp. 7–17, 1959.
[21]  I. L. Medintz, J. H. Konnert, A. R. Clapp et al., “A fluorescence resonance energy transfer-derived structure of a quantum dot-protein bioconjugate nanoassembly,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 26, pp. 9612–9617, 2004.
[22]  A. M. Dennis and G. Bao, “Quantum dot-fluorescent protein pairs as novel fluorescence resonance energy transfer probes,” Nano Letters, vol. 8, no. 5, pp. 1439–1445, 2008.
[23]  A. R. Clapp, I. L. Medintz, J. M. Mauro, B. R. Fisher, M. G. Bawendi, and H. Mattoussi, “Fluorescence resonance energy transfer between quantum dot donors and dye-labeled protein acceptors,” Journal of the American Chemical Society, vol. 126, no. 1, pp. 301–310, 2004.
[24]  A. Polozova and B. J. Litman, “Cholesterol dependent recruitment of di22:6-PC by a G protein-coupled receptor into lateral domains,” Biophysical Journal, vol. 79, no. 5, pp. 2632–2643, 2000.
[25]  M. Rehorek, N. A. Dencher, and M. P. Heyn, “Fluorescence energy transfer from diphenylhexatriene to bacteriorhodopsin in lipid vesicles,” Biophysical Journal, vol. 43, no. 1, pp. 39–45, 1983.
[26]  F. Dumas, M. M. Sperotto, M. C. Lebrun, J. F. Tocanne, and O. G. Mouritsen, “Molecular sorting of lipids by bacteriorhodopsin in dilauroylphosphatidylcholine/distearoylphosphatidylcholine lipid bilayers,” Biophysical Journal, vol. 73, no. 4, pp. 1940–1953, 1997.
[27]  M. H. Griep, K. Walczak, E. Winder, D. R. Lueking, and C. R. Friedrich, “An integrated bionanosensing method for airborne toxin detection,” in Nanobiotronics, vol. 6646, p. 664603, August 2007.
[28]  A. Rakovich, (ed Serpenguzel Ali) 736620 (SPIE).
[29]  M. Griep, E. Winder, D. Lueking, C. Friedrich, G. Mallick, and S. Kama, “Optical protein modulation via quantum dot coupling and use of a hybrid sensor protein,” Journal of Nanoscience and Nanotechnology, vol. 10, no. 9, pp. 6029–6035, 2010.
[30]  M. H. Griep, K. A. Walczak, E. M. Winder, D. R. Lueking, and C. R. Friedrich, “Quantum dot enhancement of bacteriorhodopsin-based electrodes,” Biosensors and Bioelectronics, vol. 25, no. 6, pp. 1493–1497, 2010.
[31]  P. C. Weber, D. H. Ohlendorf, J. J. Wendoloski, and F. R. Salemme, “Structural origins of high-affinity biotin binding to streptavidin,” Science, vol. 243, no. 4887, pp. 85–88, 1989.
[32]  E. Oh, M. Y. Hong, D. Lee, S. H. Nam, H. C. Yoon, and H. S. Kim, “Inhibition assay of biomolecules based on fluorescence resonance energy transfer (FRET) between quantum dots and gold nanoparticles,” Journal of the American Chemical Society, vol. 127, no. 10, pp. 3270–3271, 2005.
[33]  Y. Cui, Q. Wei, H. Park, and C. M. Lieber, “Nanowire nanosensors for highly sensitive and selective detection of biological and chemical species,” Science, vol. 293, no. 5533, pp. 1289–1292, 2001.
[34]  S. A. Darst, M. Ahlers, P. H. Meller et al., “Two-dimensional crystals of streptavidin on biotinylated lipid layers and their interactions with biotinylated macromolecules,” Biophysical Journal, vol. 59, no. 2, pp. 387–396, 1991.
[35]  T. J. Huang and J. R. Waldeisen, “Biologically inspired energy: harnessing molecular functionality towards nanosystemic design,” Nanomedicine, vol. 1, pp. 369–372, 2006.
[36]  T. Su, S. Zhong, Y. Zhang, and K. S. Hu, “Asymmetric distribution of biotin labeling on the purple membrane,” Journal of Photochemistry and Photobiology B, vol. 92, no. 2, pp. 123–127, 2008.
[37]  W. Z. Lee, G. W. Shu, J. S. Wang et al., “Recombination dynamics of luminescence in colloidal CdSe/ZnS quantum dots,” Nanotechnology, vol. 16, no. 9, pp. 1517–1521, 2005.
[38]  X. Wang, L. Qu, J. Zhang, X. Peng, and M. Xiao, “Surface-related emission in highly luminescent CdSe quantum dots,” Nano Letters, vol. 3, no. 8, pp. 1103–1106, 2003.
[39]  J. E. Halpert, J. R. Tischler, G. Nair et al., “Electrostatic formation of quantum dot/J-aggregate FRET pairs in solution,” Journal of Physical Chemistry C, vol. 113, no. 23, pp. 9986–9992, 2009.

Full-Text

comments powered by Disqus

Contact Us

service@oalib.com

QQ:3279437679

WhatsApp +8615387084133

WeChat 1538708413