Viral assembly of oriented quantum dot nanowires

被引:389
作者
Mao, CB
Flynn, CE
Hayhurst, A
Sweeney, R
Qi, JF
Georgiou, G
Iverson, B
Belcher, AM [1 ]
机构
[1] Univ Texas, Dept Chem & Biochem, Austin, TX 78712 USA
[2] Univ Texas, Dept Chem Engn, Austin, TX 78712 USA
[3] Univ Texas, Inst Cellular & Mol Biol, Austin, TX 78712 USA
[4] Univ Texas, Ctr Nano & Mol Sci & Technol, Austin, TX 78712 USA
[5] Univ Texas, Texas Mat Inst, Austin, TX 78712 USA
[6] MIT, Dept Mat Sci & Engn, Cambridge, MA 02139 USA
[7] MIT, Div Biol Engn, Cambridge, MA 02139 USA
关键词
D O I
10.1073/pnas.0832310100
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The highly organized structure of M13 bacteriophage was used as an evolved biological template for the nucleation and orientation of semiconductor nanowires. To create this organized template, peptides were selected by using a pill phage display library for their ability to nucleate ZnS or CdS nanocrystals. The successful peptides were expressed as pVIII fusion proteins into the crystalline capsid of the virus. The engineered viruses were exposed to semiconductor precursor solutions, and the resultant nanocrystals that were templated along the viruses to form nanowires were extensively characterized by using high-resolution analytical electron microscopy and photoluminescence. ZnS nanocrystals were well crystallized on the viral capsid in a hexagonal wurtzite or a cubic zinc blende structure, depending on the peptide expressed on the viral capsid. Electron diffraction patterns showed single-crystal type behavior from a polynanocrystalline area of the nanowire formed, suggesting that the nanocrystals on the virus were preferentially oriented with their [001] perpendicular to the viral surface. Peptides that specifically directed CdS nanocrystal growth were also engineered into the viral capsid to create wurtzite CdS virus-based nanowires. Lastly, heterostructured nucleation was achieved with a dual-peptide virus engineered to express two distinct peptides within the same viral capsid. This work represents a genetically controlled biological synthesis route to a semiconductor nanoscale heterostructure.
引用
收藏
页码:6946 / 6951
页数:6
相关论文
共 30 条
  • [1] Calcitic microlenses as part of the photoreceptor system in brittlestars
    Aizenberg, J
    Tkachenko, A
    Weiner, S
    Addadi, L
    Hendler, G
    [J]. NATURE, 2001, 412 (6849) : 819 - 822
  • [2] Control of crystal phase switching and orientation by soluble mollusc-shell proteins
    Belcher, AM
    Wu, XH
    Christensen, RJ
    Hansma, PK
    Stucky, GD
    Morse, DE
    [J]. NATURE, 1996, 381 (6577) : 56 - 58
  • [3] Metal-recognition by repeating polypeptides
    Brown, S
    [J]. NATURE BIOTECHNOLOGY, 1997, 15 (03) : 269 - 272
  • [4] Protein-mediated particle assembly
    Brown, S
    [J]. NANO LETTERS, 2001, 1 (07) : 391 - 394
  • [5] Silicatein filaments and subunits from a marine sponge direct the polymerization of silica and silicones in vitro
    Cha, JN
    Shimizu, K
    Zhou, Y
    Christiansen, SC
    Chmelka, BF
    Stucky, GD
    Morse, DE
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (02) : 361 - 365
  • [6] ENSHELLSEIJFFER.D, 2001, NUCLEIC ACIDS RES, V29
  • [7] Ordering nanometer-scale magnets using bacterial thread templates
    Field, M
    Smith, CJ
    Awschalom, DD
    Mendelson, NH
    Mayes, EL
    Davis, SA
    Mann, S
    [J]. APPLIED PHYSICS LETTERS, 1998, 73 (12) : 1739 - 1741
  • [8] Growth of nanowire superlattice structures for nanoscale photonics and electronics
    Gudiksen, MS
    Lauhon, LJ
    Wang, J
    Smith, DC
    Lieber, CM
    [J]. NATURE, 2002, 415 (6872) : 617 - 620
  • [9] Self-assembly and mineralization of peptide-amphiphile nanofibers
    Hartgerink, JD
    Beniash, E
    Stupp, SI
    [J]. SCIENCE, 2001, 294 (5547) : 1684 - 1688
  • [10] MODIFYING FILAMENTOUS PHAGE CAPSID - LIMITS IN THE SIZE OF THE MAJOR CAPSID PROTEIN
    IANNOLO, G
    MINENKOVA, O
    PETRUZZELLI, R
    CESARENI, G
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1995, 248 (04) : 835 - 844