Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives
Reexamination Certificate
1999-01-25
2002-08-20
Carlson, Karen Cochrane (Department: 1653)
Organic compounds -- part of the class 532-570 series
Organic compounds
Carbohydrates or derivatives
Reexamination Certificate
active
06437112
ABSTRACT:
FIELD OF THE INVENTION . . .
BACKGROUND TO THE INVENTION . . .
SUMMARY OF THE INVENTION . . .
BRIEF DESCRIPTION OF THE DRAWINGS . . .
DETAILED DESCRIPTION OF THE INVENTION . . .
DEFINITIONS . . .
STRUCTURAL UNITS . . .
DESIGN AND PRODUCTION OF THE ROD PROTEINS . . .
ASSEMBLY OF INDIVIDUAL ROD COMPONENTS INTO NANOSTRUCTURES . . .
STRUCTURAL COMPONENTS FOR SELF ASSEMBLY OF BEAMS IN VITRO . . .
APPLICATIONS . . .
KITS . . .
EXAMPLE 1: DESIGN, CONSTRUCTION AND EXPRESSION OF INTERNALLY DELETED P37 . . .
EXAMPLE 2: DESIGN, CONSTRUCTION AND EXPRESSION OF A gp37-36 CHIMER . . .
EXAMPLE 3: MUTATION OF THE GP37-36 CHIMER TO PRODUCE COMPLEMENTARY SUPPRESSORS . . .
EXAMPLE 4: DESIGN, CONSTRUCTION AND EXPRESSION OF A gp36-34 CHIMER . . .
EXAMPLE 5: ISOLATION OF THERMOLABILE PROTEINS FOR SELF-ASSEMBLY . . .
EXAMPLE 6: ASSEMBLY OF ONE-DIMENSIONAL RODS . . .
EXAMPLE 7: STAGED ASSEMBLY OF POLYGONS . . .
FIELD OF THE INVENTION
The present invention pertains to nanostructures, i.e., nanometer sized structures useful in the construction of microscopic and macroscopic structures. In particular, the present invention pertains to nanostructures based on bacteriophage T4 tail fiber proteins and variants thereof.
BACKGROUND TO THE INVENTION
While the strength of most metallic and ceramic based materials derives from the theoretical bonding strengths between their component molecules and crystallite surfaces, it is significantly limited by flaws in their crystal or glass-like structures. These flaws are usually inherent in the raw materials themselves or developed during fabrication and are often expanded due to exposure to environmental stresses.
The emerging field of nanotechnology has made the limitations of traditional materials more critical. The ability to design and produce very small structures (i.e., of nanometer dimensions) that can serve complex functions depends upon the use of appropriate materials that can be manipulated in predictable and reproducible ways, and that have the properties required for each novel application.
Biological systems serve as a paradigm for sophisticated nanostructures. Living cells fabricate proteins and combine them into structures that are perfectly formed and can resist damage in their normal environment. In some cases, intricate structures are created by a process of self-assembly, the instructions for which are built into, the component polypeptides. Finally, proteins are subject to proofreading processes that insure a high degree of quality control.
Therefore, there is a need in the art for methods and compositions that exploit these unique features of proteins to form constituents of synthetic nanostructures. The need is to design materials whose properties can be tailored to suit the particular requirements of nanometer-scale technology. Moreover, since the subunits of most macrostructural materials, ceramics, metals, fibers, etc., are based on the bonding of nanostructural subunits, the fabrication of appropriate subunits without flaws and of exact dimensions and uniformity should improve the strength and consistency of the macrostructures because the surfaces are more regular and can interact more closely over an extended area than larger, more heterogeneous material.
SUMMARY OF THE INVENTION
In one aspect, the present invention provides isolated protein building blocks for nanostructures, comprising modified tail fiber proteins of bacteriophage T4. The gp34, 36, and 37 proteins are modified in various ways to form novel rod structures with different properties. Specific internal peptide sequences may be deleted without affecting their ability to form diners and associate with their natural tail fiber partners. Alternatively, they may be modified so that they: interact only with other modified, and not native, tail fiber partners; exhibit thermolabile interactions with their partners; or contain additional functional groups that enable them to interact with heterologous binding moieties.
The present invention also encompasses fusion proteins that contain sequences from two or more different tail fiber proteins. The gp35 protein, which forms an angle joint, is modified so as to form average angles different from the natural average angle of 137° (±7°) or 156° (±12°), and to exhibit thermolabile interactions with its partners.
In another aspect, the present invention provides nanostructures comprising native and modified tail fiber proteins of bacteriophage T4. The nanostructures may be one-dimensional rods, two-dimensional polygons or open or closed sheets, or three-dimensional open cages or closed solids.
REFERENCES:
patent: 3532593 (1970-10-01), Tang
patent: 5864013 (1999-01-01), Goldberg
patent: 5877279 (1999-03-01), Goldberg
Sandmeier, 1994, Acquisition and rearrangement of sequence motifs in the evolution of bacteriophage tail fibres, Molecular Microbiology, 12(3):344-50.
Repoila et al., 1994, Genomic polymorphism in the T-even bacteriophages, EMBO J. 13(17):4181-92.
Wood et al., 1983, Long tail fibers: genes, proteins, assembly, and structure, in Bacteriophage T4, Mathews, Kutter, Mosig and Berget (eds.), American Society of Microbiology, Washington, D.C., pp. 259-269.
Monod et al., 1997, The genome of the pseudo t-even bacteriophages, a diverse group that resembles T4, J. Mol. Biol. 267: 237-49.
Tétart et al., 2001, Phylogeny of the major head and tail genes of the wide-ranging T4-type bacteriophages, Journal of Bacteriology 183(1):358-66.
Hahn et al., 1989, Organization of the bacteriophage T4 genome between map positions 150.745 and 145.824, Nucleic Acids Res. 17:6729.
Robertson et al., 1991, Use of group-specific primers and the polymerase chain reaction for the detection and identification of luteoviruses, J. Gen. Virol. 72:1473-77.
Langeveld et al., 1991, Identification of potyviruses using the polymerase chain reaction with degenerate primers, J. Gen. Virol. 72:1531-41.
Montag et al., 1987, Receptor-recognizing proteins of T-even type bacteriophages. Constant and hypervariable regions and an unusual case of evolution, J. Mol. Biol. 196 (1), 165-74.
Montag et al., 1990, Receptor-recognizing proteins of T-even type bacteriophages. The receptor-recognizing area of proteins 37 of phages T4 Tula and Tulb, J. Mol. Biol. 216 (2), 327-34.
Riede et al., 1984 DNA sequence heterogeneity in the genes of T-even typeEscherichia coliphages encoding the receptor recognizing protein of the long tail, Mol. Gen. Genet. 195 (1-2), 144-52.
Snyder and Wood, Jul. 1989, Genetic Definition of Two Functional Elements in a Bacteriophage T4 Host-Range “Cassette”, Genetics 122, 471-479.
Ackermann and Krisch, 1997, “A Catalogue of T-4 Type Bacteriophages”, Arch. Virol. 142:2329-2345.
Beckendorf et al., 1973, “Structure of Bacteriophage T4 Genes 37 and 38”, J. Mol. Biol. 73:17-35.
Beckendorf, 1973, “Structure of the Distal Half of the Bacteriophage T4 Tail Fiber”, J. Mol. Biol. 73:37-53.
Haggård-Ljungquist et al., 1992, “DNA Sequences of the Tail Fiber Genes of Bacteriophage P2: Evidence of Horizontal Transfer for Tail Fiber Genes among Unrelated Bacteriophages”, J. Bacteriol. 174:1462-1477.
Henning and Hashemolhosseini, 1994, “Receptor Recognition by T-Even-Type Coliphages”, Chapter 23 in Molecular Biology of Bacteriophage T4, Karam, ed., American Society for Microbiology, Washington, D.C., pp. 291-298.
Riede et al., 1986, “DNA Sequence of the Tail Fiber Genes 37, Encoding the Receptor Recognizing Part of the Fiber, of Bacteriophages T2 and K3”, J. Mol. Biol. 191:255-266.
Riede et al., 1985, “The Nucleotide Sequences of the Tail Fiber Gene 36 of Bacteriophage T2 and of Genes 36 of the T TypeEscherichia coliPhages K3 and Ox2”, Nucl. Acids Res. 13:605-616.
Russell, 1974, “Comparative Genetics of the T-Even Bacteriophages”, Genetics 78:967-988.
Bella et al., 1994, “Crystal and molecular structure of a collagen-like peptide at 1.9Å resolution”, Science 226:75-81.
T.E. Creighton (ed.), 1984,Proteins, Structures and Molecular Principles, W.H. Freeman & Co, NY, pp. 25-28.
Earnshaw et al., 1979, “The distal half of the tail fibre of the bacteriophage T4 ri
Carlson Karen Cochrane
NanoFrames, LLC
Pennie & Edmonds LLP
LandOfFree
Materials for the production of nanometer structures and use... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Materials for the production of nanometer structures and use..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Materials for the production of nanometer structures and use... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-2941667