Self-Assembling Light-Harvesting Systems from Synthetically Modified Tobacco Mosaic Virus Coat Proteins.

Department of Chemistry, University of California, Berkeley, California 94720-1460, USA.
Journal of the American Chemical Society (Impact Factor: 11.44). 04/2007; 129(11):3104-9. DOI: 10.1021/ja063887t
Source: PubMed

ABSTRACT A new protein-based approach has been developed for the construction of light-harvesting systems through self-assembly. The building blocks were prepared by attaching fluorescent chromophores to cysteine residues introduced on tobacco mosaic virus coat protein monomers. When placed under the appropriate buffer conditions, these conjugates could be assembled into stacks of disks or into rods that reached hundreds of nanometers in length. Characterization of the system using fluorescence spectroscopy indicated that efficient energy transfer could be achieved from large numbers of donor chromophores to a single acceptor. Energy transfer is proposed to occur through direct donor-acceptor interactions, although degenerate donor-to-donor transfer events are also possible. Three-chromophore systems were also prepared to achieve broad spectrum light collection with over 90% overall efficiency. Through the combination of self-organizing biological structures and synthetic building blocks, a highly tunable new method has emerged for the construction of photovoltaic device components.

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    • "Some shapes are quite sophisticated; for example, T4 and T7 phages possess an icosahedral head and a long tail connected through a cylindrical body [170]. Over the last two decades, the biochemical landscape of the phage structure has been greatly expanded through genetic engineering [179] [180] [181] [182] and site-specific organic synthesis approaches [183] [184] [185] [186]. Through "
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    02/2014; 2014:814208. DOI:10.1155/2014/814208
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    • "Researchers have begun to harness this extraordinary assembly capability to make a variety of devices by integrating peptides or proteins which are able to bind technologically significant materials into the structural proteins of viruses. This approach has allowed the realization of unique device geometries, as well as the opportunity for enhanced performance and functionality [1] [2] [3] [4] [5]. One area of viral-assisted assembly that has yet to be fully explored is the formation of core–shell materials. "
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    Materials Letters 12/2012; 89:347–350. DOI:10.1016/j.matlet.2012.09.001 · 2.27 Impact Factor
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    • "The capacity for biological macromolecules to self-assemble into structurally well-defined aggregates is of particular interest to technologists in the development of nanostructured devices and to molecular biologists in the development of drug delivery and imaging systems (Lowe, 2000; Wu & Payne, 2004). As such, plant virus capsid proteins (CPs) have been studied for their ability to form multilayered arrays (Steinmetz et al., 2008), nanotubes (Wang et al., 2008), light-harvesting systems (Miller et al., 2007) and diagnostic imaging devices (Gonzalez et al., 2009), and for epitope display (Smith et al., 2009). (For more general reviews, see Douglas & Young, 2006; Fischlechner & Donath, 2007; Manchester & Singh, 2006; Ren et al., 2010; Singh et al., 2006; and Young et al., 2008). "
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