Article

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.

1 Follower
 · 
86 Views
  • Source
    • "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 "
    [Show abstract] [Hide abstract]
    ABSTRACT: Targeted delivery systems of nanobiomaterials are necessary to be developed for the diagnosis and treatment of cancer. Nanobiomaterials can be engineered to recognize cancer-specific receptors at the cellular levels and to deliver anticancer drugs into the diseased sites. In particular, nanobiomaterial-based nanocarriers, so-called nanoplatforms, are the design of the targeted delivery systems such as liposomes, polymeric nanoparticles/micelles, nanoconjugates, norganic materials, carbon-based nanobiomaterials, and bioinspired phage system, which are based on the nanosize of 1-100 nm in diameter. In this review, the design and the application of these nanoplatforms are discussed at the cellular levels as well as in the clinics. We believe that this review can offer recent advances in the targeted delivery systems of nanobiomaterials regarding in vitro and in vivo applications and the translation of nanobiomaterials to nanomedicine in anticancer therapy.
    02/2014; 2014:814208. DOI:10.1155/2014/814208
  • Source
    • "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. "
    [Show abstract] [Hide abstract]
    ABSTRACT: Individual viral-templated Au/CdSe core–shell nanowires were synthesized and electrically characterized at room temperature. The Au nanowire cores were constructed using a genetically-modified filamentous M13 bacteriophage as a scaffold. Au nanoparticles were selectively bound to the viruses and used as seeds for electroless deposition, forming continuous Au nanowires. The nanocrystalline CdSe shell material which formed a coaxial heterojunction with the Au nanowire was created by electrodeposition. Electrical characterization of the Au nanowires revealed resistance variations associated with the viral-templated assembly process. The photoelectrical response of the core–shell nanowires was used to assess the interaction between the two component materials. A correlation was found between the dark current of the Au/CdSe core–shell nanowire and the magnitude of the collected photocurrent.
    Materials Letters 12/2012; 89:347–350. DOI:10.1016/j.matlet.2012.09.001 · 2.27 Impact Factor
  • Source
    • "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). "
    [Show abstract] [Hide abstract]
    ABSTRACT: An important property of some spherical plant viruses is their ability to reassemble in vitro from native capsid protein (CP) and RNA into infectious virus-like particles (VLPs). Virions of cucumber mosaic virus (CMV) are stabilized by protein-RNA interactions and the nucleic acid is essential for assembly. This study demonstrated that VLPs will form in the presence of both ssDNA and dsDNA oligonucleotides, and with a lower size limit of 20 nt. Based on urea disruption assays, assembled VLPs from CMV CP and RNA (termed ReCMV) exhibited a level of stability similar to that of virions purified from plants, whilst VLPs from CMV CP and a 20mer exhibited comparable or greater stability. Fluorescent labelling of VLPs was achieved by the encapsidation of an Alexa Fluor 488-labelled 45mer oligonucleotide (ReCMV-Alexa488-45) and confirmed by transmission electron and confocal microscopy. Using ssDNA as a nucleating factor, encapsidation of fluorescently labelled streptavidin (53 kDa) conjugated to a biotinylated oligonucleotide was observed. The biological activity and stability of ReCMV and ReCMV-Alexa488-45 was confirmed in infectivity assays and insect vector feeding assays. This work demonstrates the utility of CMV CP as a protein cage for use in the growing repertoire of nanotechnological applications.
    Journal of General Virology 01/2012; 93(Pt 5):1120-6. DOI:10.1099/vir.0.040170-0 · 3.53 Impact Factor
Show more