WO2006130150A2 - Nanotubes de carbone a simple paroi fonctionnalises - Google Patents

Nanotubes de carbone a simple paroi fonctionnalises Download PDF

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Publication number
WO2006130150A2
WO2006130150A2 PCT/US2005/022413 US2005022413W WO2006130150A2 WO 2006130150 A2 WO2006130150 A2 WO 2006130150A2 US 2005022413 W US2005022413 W US 2005022413W WO 2006130150 A2 WO2006130150 A2 WO 2006130150A2
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Prior art keywords
walled carbon
single walled
fibrils
less
carbon nanotubes
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PCT/US2005/022413
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WO2006130150A9 (fr
WO2006130150A3 (fr
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Robert Hoch
Alan Fischer
Howard Tennent
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Hyperion Catalysis International, Inc.
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Priority to CA002571575A priority Critical patent/CA2571575A1/fr
Priority to AU2005332329A priority patent/AU2005332329A1/en
Priority to EP05857879A priority patent/EP1776125A4/fr
Priority to JP2007519302A priority patent/JP2008513318A/ja
Publication of WO2006130150A2 publication Critical patent/WO2006130150A2/fr
Publication of WO2006130150A3 publication Critical patent/WO2006130150A3/fr
Publication of WO2006130150A9 publication Critical patent/WO2006130150A9/fr

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    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
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    • B01J31/00—Catalysts comprising hydrides, coordination complexes or organic compounds
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    • C01B—NON-METALLIC ELEMENTS; COMPOUNDS THEREOF; METALLOIDS OR COMPOUNDS THEREOF NOT COVERED BY SUBCLASS C01C
    • C01B32/00—Carbon; Compounds thereof
    • C01B32/15—Nano-sized carbon materials
    • C01B32/158—Carbon nanotubes
    • C01B32/168—After-treatment
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
    • B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
    • B01J21/00—Catalysts comprising the elements, oxides, or hydroxides of magnesium, boron, aluminium, carbon, silicon, titanium, zirconium, or hafnium
    • B01J21/18—Carbon
    • B01J21/185—Carbon nanotubes
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B82—NANOTECHNOLOGY
    • B82B—NANOSTRUCTURES FORMED BY MANIPULATION OF INDIVIDUAL ATOMS, MOLECULES, OR LIMITED COLLECTIONS OF ATOMS OR MOLECULES AS DISCRETE UNITS; MANUFACTURE OR TREATMENT THEREOF
    • B82B1/00—Nanostructures formed by manipulation of individual atoms or molecules, or limited collections of atoms or molecules as discrete units
    • B82B1/008—Nanostructures not provided for in groups B82B1/001 - B82B1/007
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B82—NANOTECHNOLOGY
    • B82B—NANOSTRUCTURES FORMED BY MANIPULATION OF INDIVIDUAL ATOMS, MOLECULES, OR LIMITED COLLECTIONS OF ATOMS OR MOLECULES AS DISCRETE UNITS; MANUFACTURE OR TREATMENT THEREOF
    • B82B3/00—Manufacture or treatment of nanostructures by manipulation of individual atoms or molecules, or limited collections of atoms or molecules as discrete units
    • B82B3/0061—Methods for manipulating nanostructures
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B82—NANOTECHNOLOGY
    • B82B—NANOSTRUCTURES FORMED BY MANIPULATION OF INDIVIDUAL ATOMS, MOLECULES, OR LIMITED COLLECTIONS OF ATOMS OR MOLECULES AS DISCRETE UNITS; MANUFACTURE OR TREATMENT THEREOF
    • B82B3/00—Manufacture or treatment of nanostructures by manipulation of individual atoms or molecules, or limited collections of atoms or molecules as discrete units
    • B82B3/0095—Manufacture or treatments or nanostructures not provided for in groups B82B3/0009 - B82B3/009
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B82—NANOTECHNOLOGY
    • B82Y—SPECIFIC USES OR APPLICATIONS OF NANOSTRUCTURES; MEASUREMENT OR ANALYSIS OF NANOSTRUCTURES; MANUFACTURE OR TREATMENT OF NANOSTRUCTURES
    • B82Y30/00—Nanotechnology for materials or surface science, e.g. nanocomposites
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B82—NANOTECHNOLOGY
    • B82Y—SPECIFIC USES OR APPLICATIONS OF NANOSTRUCTURES; MEASUREMENT OR ANALYSIS OF NANOSTRUCTURES; MANUFACTURE OR TREATMENT OF NANOSTRUCTURES
    • B82Y40/00—Manufacture or treatment of nanostructures
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    • C01—INORGANIC CHEMISTRY
    • C01B—NON-METALLIC ELEMENTS; COMPOUNDS THEREOF; METALLOIDS OR COMPOUNDS THEREOF NOT COVERED BY SUBCLASS C01C
    • C01B32/00—Carbon; Compounds thereof
    • C01B32/15—Nano-sized carbon materials
    • C01B32/158—Carbon nanotubes
    • C01B32/168—After-treatment
    • C01B32/174—Derivatisation; Solubilisation; Dispersion in solvents
    • C—CHEMISTRY; METALLURGY
    • C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
    • C08K—Use of inorganic or non-macromolecular organic substances as compounding ingredients
    • C08K3/00—Use of inorganic substances as compounding ingredients
    • C08K3/02—Elements
    • C08K3/04—Carbon
    • C08K3/041—Carbon nanotubes
    • D—TEXTILES; PAPER
    • D01—NATURAL OR MAN-MADE THREADS OR FIBRES; SPINNING
    • D01F—CHEMICAL FEATURES IN THE MANUFACTURE OF ARTIFICIAL FILAMENTS, THREADS, FIBRES, BRISTLES OR RIBBONS; APPARATUS SPECIALLY ADAPTED FOR THE MANUFACTURE OF CARBON FILAMENTS
    • D01F11/00—Chemical after-treatment of artificial filaments or the like during manufacture
    • D01F11/10—Chemical after-treatment of artificial filaments or the like during manufacture of carbon
    • D01F11/12—Chemical after-treatment of artificial filaments or the like during manufacture of carbon with inorganic substances ; Intercalation
    • D—TEXTILES; PAPER
    • D01—NATURAL OR MAN-MADE THREADS OR FIBRES; SPINNING
    • D01F—CHEMICAL FEATURES IN THE MANUFACTURE OF ARTIFICIAL FILAMENTS, THREADS, FIBRES, BRISTLES OR RIBBONS; APPARATUS SPECIALLY ADAPTED FOR THE MANUFACTURE OF CARBON FILAMENTS
    • D01F11/00—Chemical after-treatment of artificial filaments or the like during manufacture
    • D01F11/10—Chemical after-treatment of artificial filaments or the like during manufacture of carbon
    • D01F11/14—Chemical after-treatment of artificial filaments or the like during manufacture of carbon with organic compounds, e.g. macromolecular compounds
    • C—CHEMISTRY; METALLURGY
    • C01—INORGANIC CHEMISTRY
    • C01B—NON-METALLIC ELEMENTS; COMPOUNDS THEREOF; METALLOIDS OR COMPOUNDS THEREOF NOT COVERED BY SUBCLASS C01C
    • C01B2202/00—Structure or properties of carbon nanotubes
    • C01B2202/02—Single-walled nanotubes
    • C—CHEMISTRY; METALLURGY
    • C01—INORGANIC CHEMISTRY
    • C01B—NON-METALLIC ELEMENTS; COMPOUNDS THEREOF; METALLOIDS OR COMPOUNDS THEREOF NOT COVERED BY SUBCLASS C01C
    • C01B2202/00—Structure or properties of carbon nanotubes
    • C01B2202/20—Nanotubes characterized by their properties
    • C01B2202/36—Diameter
    • H—ELECTRICITY
    • H01—ELECTRIC ELEMENTS
    • H01M—PROCESSES OR MEANS, e.g. BATTERIES, FOR THE DIRECT CONVERSION OF CHEMICAL ENERGY INTO ELECTRICAL ENERGY
    • H01M4/00—Electrodes
    • H01M4/02—Electrodes composed of, or comprising, active material
    • H01M4/36—Selection of substances as active materials, active masses, active liquids
    • H01M4/58—Selection of substances as active materials, active masses, active liquids of inorganic compounds other than oxides or hydroxides, e.g. sulfides, selenides, tellurides, halogenides or LiCoFy; of polyanionic structures, e.g. phosphates, silicates or borates
    • H01M4/583—Carbonaceous material, e.g. graphite-intercalation compounds or CFx
    • H01M4/587—Carbonaceous material, e.g. graphite-intercalation compounds or CFx for inserting or intercalating light metals
    • H—ELECTRICITY
    • H01—ELECTRIC ELEMENTS
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    • H01M4/00—Electrodes
    • H01M4/02—Electrodes composed of, or comprising, active material
    • H01M4/62—Selection of inactive substances as ingredients for active masses, e.g. binders, fillers
    • H01M4/624—Electric conductive fillers
    • H01M4/625—Carbon or graphite
    • H—ELECTRICITY
    • H01—ELECTRIC ELEMENTS
    • H01M—PROCESSES OR MEANS, e.g. BATTERIES, FOR THE DIRECT CONVERSION OF CHEMICAL ENERGY INTO ELECTRICAL ENERGY
    • H01M8/00—Fuel cells; Manufacture thereof
    • H01M8/18—Regenerative fuel cells, e.g. redox flow batteries or secondary fuel cells
    • Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
    • Y02E—REDUCTION OF GREENHOUSE GAS [GHG] EMISSIONS, RELATED TO ENERGY GENERATION, TRANSMISSION OR DISTRIBUTION
    • Y02E60/00—Enabling technologies; Technologies with a potential or indirect contribution to GHG emissions mitigation
    • Y02E60/10—Energy storage using batteries
    • Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
    • Y02E—REDUCTION OF GREENHOUSE GAS [GHG] EMISSIONS, RELATED TO ENERGY GENERATION, TRANSMISSION OR DISTRIBUTION
    • Y02E60/00—Enabling technologies; Technologies with a potential or indirect contribution to GHG emissions mitigation
    • Y02E60/30—Hydrogen technology
    • Y02E60/50—Fuel cells

Definitions

  • the invention relates broadly to graphitic nanotubes, which includes tubular fullerenes (commonly called "buckytubes") and fibrils, which are functional ized by chemical substitution or by adsorption of functional moieties. More specifically the invention relates to single walled carbon nanotubes which are uniformly or non-uniformly substituted with chemical moieties or upon which certain cyclic compounds are adsorbed and to complex structures comprised of such functionalized fibrils linked to one another. The invention also relates to methods of introducing functional groups onto the surface of single walled carbon nanotubes.
  • This invention lies in the field of submicron graphitic fibrils, sometimes called vapor grown carbon fibers.
  • Carbon fibrils are vermicular carbon deposits having diameters less than 1.0 ⁇ , preferably less than 0.5 ⁇ , and even more preferably less than 0.2 ⁇ . They exist in a variety of forms and have been prepared through the catalytic decomposition of various carbon-containing gases at metal surfaces. Such vermicular carbon deposits have been observed almost since the advent of electron microscopy.
  • a good early survey and reference is found in Baker and Harris, Chemistry and Physics of Carbon. Walker and Thrower ed., Vol. 14, 1978, p. 83, hereby incorporated by reference. See also, Rodriguez, N., J. Mater. Research. Vol. 8, p. 3233 (1993), hereby incorporated by reference.
  • Endo et al. see Obelin, A. and Endo, M., J. of Crystal Growth. Vol.
  • Tennent U.S. Patent No. 4,663,230, hereby incorporated by reference, succeeded in growing cylindrical ordered graphite cores, uncontaminated with pyrolytic carbon.
  • the Tennent invention provided access to smaller diameter fibrils, typically 35 to 700 A (0.0035 to 0.070 ⁇ ) and to an ordered, "as grown" graphitic surface. Fibrillar carbons of less perfect structure, but also without a pyrolytic carbon outer layer have also been grown.
  • the fibrils, buckytubes and nanofibers that are functionalized in this application are distinguishable from continuous carbon fibers commercially available as reinforcement materials.
  • continuous carbon fibers which have, desirably large, but unavoidably finite aspect ratios
  • continuous carbon fibers have aspect ratios (L/D) of at least 10 4 and often 10 6 or more.
  • the diameter of continuous fibers is also far larger than that of fibrils, being always >1.0 ⁇ and typically 5 to 7 ⁇ .
  • Continuous carbon fibers are made by the pyrolysis of organic precursor fibers, usually rayon, polyacrylonitrile (PAN) and pitch. Thus, they may include heteroatoms within their structure.
  • PAN polyacrylonitrile
  • the graphitic nature of "as made" continuous carbon fibers varies, but they may be subjected to a subsequent graphitization step. Differences in degree of graphitization, orientation and crystallinity of graphite planes, if they are present, the potential presence of heteroatoms and even the absolute difference in substrate diameter make experience with continuous fibers poor predictors of nanofiber chemistry.
  • 4,663,230 describes carbon fibrils that are free of a continuous thermal carbon overcoat and have multiple graphitic outer layers that are substantially parallel to the fibril axis. As such they may be characterized as having their c- axes, the axes which are perpendicular to the tangents of the curved layers of graphite, substantially perpendicular to their cylindrical axes. They generally have diameters no greater than O.l ⁇ and length to diameter ratios of at least 5. Desirably they are substantially free of a continuous thermal carbon overcoat, i.e., pyrolytically deposited carbon resulting from thermal cracking of the gas feed used to prepare them. [0009] Tennent, et al., U.S. Patent No.
  • Carbon nanotubes of a morphology similar to the catalytically grown fibrils described above have been grown in a high temperature carbon arc (Iijima, Nature 354 56 1991). It is now generally accepted (Weaver, Science 265 1994) that these arc-grown nanofibers have the same morphology as the earlier catalytically grown fibrils of Tennent. Arc grown carbon nanofibers are also useful in the invention.
  • Moy disclosed a process for producing hollow, single-walled carbon nanotubes by catalytic decomposition of one or more gaseous carbon compounds by first forming a gas phase mixture carbon feed stock gas comprising one or more gaseous carbon compounds, each having one to six carbon atoms and only H, O, N, S or Cl as hetero atoms, optionally admixed with hydrogen, and a gas phase metal containing compound which is unstable under reaction conditions for said decomposition, and which forms a metal containing catalyst which acts as a decomposition catalyst under reaction conditions; and then conducting said decomposition reaction under decomposition reaction conditions, thereby producing said nanotubes.
  • a gas phase mixture carbon feed stock gas comprising one or more gaseous carbon compounds, each having one to six carbon atoms and only H, O, N, S or Cl as hetero atoms, optionally admixed with hydrogen, and a gas phase metal containing compound which is unstable under reaction conditions for said decomposition, and which forms a metal containing catalyst which acts as a de
  • the invention relates to a gas phase reaction in which a gas phase metal containing compound is introduced into a reaction mixture also containing a gaseous carbon source.
  • the carbon source is typically a Ci through C ⁇ compound having as hetero atoms H, O, N, S or Cl, optionally mixed with hydrogen.
  • Carbon monoxide or carbon monoxide and hydrogen is a preferred carbon feedstock.
  • Increased reaction zone temperatures of approximately 400 0 C. to 1300 0 C. and pressures of between about 0 and about 100 p.s.i.g., are believed to cause decomposition of the gas phase metal containing compound to a metal containing catalyst. Decomposition may be to the atomic metal or to a partially decomposed intermediate species.
  • the metal containing catalysts (1) catalyze CO decomposition and (2) catalyze SWNT formation.
  • the invention also relates to forming SWNT via catalytic decomposition of a carbon compound.
  • the invention of U.S. Patent No. 6,221,330 may in some embodiments Attorney DXket No. 100647-03591
  • An advantage of an aerosol method for producing SWNT is that it will be possible to produce catalyst particles of uniform size and scale such a method for efficient and continuous commercial or industrial production.
  • the previously discussed electric arc discharge and laser deposition methods cannot economically be scaled up for such commercial or industrial production.
  • metal containing compounds useful in the invention include metal carbonyls, metal acetyl acetonates, and other materials which under decomposition conditions can be introduced as a vapor which decomposes to form an unsupported metal catalyst.
  • Catalytically active metals include Fe, Co, Mn, Ni and Mo.
  • Molybdenum carbonyls and Iron carbonyls are the preferred metal containing compounds which can be decomposed under reaction conditions to form vapor phase catalyst. Solid forms of these metal carbonyls may be delivered to a pretreatment zone where they are vaporized, thereby becoming the vapor phase precursor of the catalyst. It was found that two methods may be employed to form SWNT on unsupported catalysts. [0017] The first method is the direct injection of volatile catalyst. The direct injection method is described is U.S. Application Ser. No. 08/459,534, incorporated herein by reference.
  • the second method uses a vaporizer to introduce the metal containing compound (FIG. 12).
  • the vaporizer 10 shown at FIG. 12, comprises a quartz thermowell 20 having a seal 24 about 1 " from its bottom to form a second compartment. This compartment has two 1/4" holes 26 which are open and exposed to the reactant gases.
  • the catalyst is placed into this compartment, and then vaporized at any desired temperature using a vaporizer furnace 32. This furnace is controlled using a first thermocouple 22.
  • a metal containing compound preferably a metal carbonyl
  • reactant gases CO or CO/H.sub.2 sweep the precursor into the reaction zone 34, which is controlled separately by a reaction zone furnace 38 and second thermocouple 42.
  • the metal containing compound is decomposed either partially to an intermediate species or completely to metal atoms. These intermediate species and/or metal atoms coalesce to larger aggregate particles which are the actual catalyst. The particle then grows to the correct size to both catalyze the decomposition of CO and promote SWNT growth.
  • the catalyst particles and the resultant carbon forms are collected on the quartz wool plug 36. Rate of growth of the particles depends on the concentration of the gas phase metal containing intermediate species. This concentration is determined by the vapor pressure (and therefore the temperature) in the vaporizer. If the concentration is too high, particle growth is too rapid, and structures other than SWNT are grown (e.g., MWNT, amorphous carbon, onions, etc.). All of the contents of U.S. Patent No. 6,221,330, including the Examples described therein, are hereby incorporated by reference.
  • Supported metal catalysts for formation of SWNT are also known. Smalley
  • Fibrils have also been oxidized non-uniformly by treatment with nitric acid.
  • Polymer Chem. 30 (1)420(1990) prepared derivatives of oxidized fibrils in order to demonstrate that the surface comprised a variety of oxidized groups.
  • Fig. 1 is a graphical representation of an assay of BSA binding to plain fibrils, carboxy fibrils, and PEG-modified fibrils.
  • Fig. 2 is a graphical representation of an assay of ⁇ -lactoglobulin binding to carboxy fibrils and PEG-modified fibrils prepared by two different methods.
  • Fig. 3 is a graphical representation of the elution profile of bovine serum albumin (BSA) on a tertiary amine fibril column.
  • BSA bovine serum albumin
  • Fig. 4 is a graphical representation of the elution profile of BSA on a quaternary amine fibril column.
  • Fig. 5 is the reaction sequence for the preparation lysine-based dendrimeric fibrils.
  • Fig. 6 is a graphical representation of cyclic voltammograms demonstrating the use of iron phthalocyanine modified fibrils in a flow cell.
  • Fig. 7 is the reaction sequence for the preparation of bifunctional fibrils by the addition of N ⁇ -(tert-butoxycarbonyl)-L-lysine.
  • Fig. 8 is a graphical representation of the results of the synthesis of ethyl butyrate using fibril-immobilized lipase.
  • Fig. 9 is a graphical representation of the results of separation of alkaline phosphatase (AP) from a mixture of AP and ⁇ -galactosidase ( ⁇ G) using AP inhibitor- modified fibrils.
  • AP alkaline phosphatase
  • ⁇ G ⁇ -galactosidase
  • Fig. 10 is a graphical representation of the results of separation of ⁇ G from a mixture of AP and ⁇ G using ⁇ G-modified fibrils.
  • Fig. 11 illustrates a reactor capable of producing single walled carbon nanotubes.
  • Fig. 12 illustrates the vaporizer component of the reactor described in Fig. 11.
  • compositions which broadly have the formula
  • n is an integer
  • L is a number less than O.ln
  • m is a number less than 0.5n
  • each of R is the same and is selected from SO 3 H 3 COOH, NH 2 , OH, R'CHOH, CHO, CN, COCl, halide, COSH, SH, COOR', SR', SiR' 3 , Si(OR') y R' 3-y , Si(O- SiR' 2 )OR', R", Li, A1R' 2 , Hg-X, TlZ 2 and Mg-X, y is an integer equal to or less than 3,
  • R' is hydrogen, alkyl, aryl, cycloalkyl, or aralkyl, cycloaryl, or poly(alkylether),
  • R" is fluoroalkyl, fluoroaryl, fluorocycloalkyl, fluoroaralkyl or cycloaryl,
  • X is halide
  • Z is carboxylate or trifluoroacetate.
  • the carbon atoms, C n are surface carbons of a substantially cylindrical, graphitic nanotube of substantially constant diameter.
  • the nanotubes include those having a Attorney Dc55ket No. 100647-03591 10 length to diameter ratio of greater than 5 and a diameter of less than 0.5 ⁇ , preferably less than O.l ⁇ .
  • the nanotubes can also be substantially cylindrical, graphitic nanotubes which are substantially free of pyrolytically deposited carbon, more preferably those characterized by having a projection of the graphite layers on the fibril axis which extends for a distance of at least two fibril diameters and/or those having cylindrical graphitic sheets whose c-axes are substantially perpendicular to their cylindrical axis.
  • carbon atoms, C n are surface carbons of a substantially cylindrical, single walled carbon nanotube of substantially constant diameter or having diameter less than 5 nanometers. Most preferably, the carbon atoms C n are surface atoms of single walled carbon nanotube having a diameter less than 5 nanometers. These compositions are uniform in that each of R is the same.
  • Non-uniformly substituted nanotubes are also prepared. These include compositions of the formula
  • n, L, m, R and the nanotube itself are as defined above, provided that each of R does not contain oxygen, or, if each of R is an oxygen-containing group COOH is not present.
  • n, L, m, R and R' have the same meaning as above and the carbon atoms are surface carbon atoms of a fishbone fibril having a length to diameter ratio greater than 5 or are carbon atons of a single walled carbon nanotube having a diameter less than 5 nanometers, are also included within the invention. These may be uniformly or non-uniformly substituted.
  • the nanotubes are free of thermal overcoat and have diameters less than ⁇ .5 ⁇ .
  • the carbon atoms, C n are surface carbons of a substantially cylindrical, graphitic nanotube of substantially constant diameter.
  • the nanotubes have a length to diameter ratio of greater than 5 and a diameter of less than 0.5 ⁇ , preferably less than O.l ⁇ .
  • the nanotubes may be nanotubes which are substantially free of pyrolytically deposited carbon. Additionally, the nanotubes are those in which the Attorney DSHcet No. 100647-03591 11 projection of the graphite layers on the fibril axes extends for a distance of at least two fibril diameters and/or those having cylindrical graphitic sheets whose c-axes are substantially perpendicular their cylindrical axis.
  • carbon atoms, C n are surface carbons of a substantially cylindrical, single walled carbon nanotube of substantially constant diameter or having diameter less than 5 nanometers. Most preferably, the carbon atoms C n are surface atoms of single walled carbon nanotube having a diameter less than 5 nanometers.
  • C n are reacted.
  • edge or basal plane carbons of lower, interior layers of the nanotube may be exposed.
  • surface carbon includes all the carbons, basal plane and edge, of the outermost layer of the nanotube, as well as carbons, both basal plane and/or edge, of lower layers that may be exposed at defect sites of the outermost layer.
  • the edge carbons are reactive and must contain some heteroatom or group to satisfy carbon valency.
  • the substituted nanotubes described above may advantageously be further functionalized. Such compositions include compositions of the formula
  • A is selected from
  • Y is an appropriate functional group of a protein, a peptide, an amino acid, an enzyme, an antibody, a nucleotide, an oligonucleotide, an antigen, or an enzyme substrate, enzyme inhibitor or the transition state analog of an enzyme substrate or is selected from R'- OH, R'-NR' 2 , R'SH, R'CHO, R'CN, R'X, R 1 N + (RO 3 X " R'SiR' 3 , R'Si ⁇ OR') y R' 3-y , R 5 Si(O- SiR' 2 )OR', R'-R", R'-N-CO, (C 2 H 4 O) W -H, ⁇ C 3 H 6 O) W H, (C 2 H 4 O) W -R', (C 3 H 6 O) W -R', Attorney ⁇ Tket No. 100647-03591 12
  • the carbon atoms, C n are surface carbons of a substantially cylindrical, graphitic nanotube of substantially constant diameter.
  • the nanotubes include those having a length to diameter ratio of greater than 5 and a diameter of less than O.l ⁇ , preferably less than 0.05 ⁇ .
  • the nanotubes can also be substantially cylindrical, graphitic nanotubes which are substantially free of pyrolytically deposited carbon. More preferably they are characterized by having a projection of the graphite layers on the fibril axes which extends for a distance of at least two fibril diameters and/or they are comprised of cylindrical graphitic sheets whose c-axes are substantially perpendicular to their cylindrical axes.
  • the nanotubes are free of thermal overcoat and have diameters less than 0.5 ⁇ .
  • the nanotubes may be substantially cylindrical, single walled carbon nanotube of substantially constant diameter or having diameter less than 5 nanometers.
  • the carbon atoms C n are surface atoms of single walled carbon nanotube having a diameter less than 5 nanometers.
  • [C n H L ⁇ [R'-R] m may also be functionalized to produce compositions having the formula
  • C n are surface carbons of a substantially cylindrical, graphitic nanotube of substantially constant diameter.
  • the nanotubes include those having a length to diameter ratio of greater than 5 and a diameter of less than 0.5 ⁇ , preferably less than O.l ⁇ .
  • the nanotubes can also be substantially cylindrical, graphitic nanotubes which are substantially free of pyrolytically deposited carbon.
  • the nanotubes are free of thermal overcoat and have diameters less than 0.5 ⁇ .
  • the nanotubes may be substantially cylindrical, single walled carbon nanotube of substantially constant diameter or having diameter less than 5 nanometers.
  • the carbon atoms C n are surface atoms of single walled carbon nanotube having a diameter less than 5 nanometers.
  • compositions of the invention also include nanotubes upon which certain cyclic compounds are adsorbed. These include compositions of matter of the formula
  • n is an integer
  • L is a number less than O.ln
  • m is less than 0.5n
  • a is zero or a number less than 10
  • X is a polynuclear aromatic, polyheteronuclear aromatic or metallopolyheteronuclear aromatic moiety or is a planar metal tetrathiooxalate
  • R is as recited above.
  • the carbon atoms, C n are surface carbons of a substantially cylindrical, graphitic nanotube of substantially constant diameter.
  • the nanotubes include those having a length to diameter ratio of greater than 5 and a diameter of less than 0.5 ⁇ , preferably less than 0.1 ⁇ .
  • the nanotubes can also be substantially cylindrical, graphitic nanotubes which are substantially free of pyrolytically deposited carbon and more preferably those characterized by having a projection of the graphite layers on said fibril axes which extend for a distance of at least two fibril diameters and/or those having cylindrical graphitic sheets whose c-axes are substantially perpendicular to their cylindrical axes.
  • the nanotubes are free of thermal overcoat and have diameters less than 0.5 ⁇ .
  • the nanotubes may be substantially cylindrical, single walled carbon nanotube of substantially constant diameter or having diameter less than 5 nanometers.
  • the carbon atoms C n are surface atoms of single walled carbon nanotube having a diameter less than 5 nanometers.
  • Preferred cyclic compounds are planar macrocycles as described on p. 76 of
  • compositions of the invention also include single walled carbon nanotubes having diameters less than 5 nanometers upon which certain planar aromatic compounds are adsorbed on the walls of the single walled carbon nanotubes. If the adsorbed molecules are themselves functionalized then the sidewalls are effectively functionalized without comprising their physical structure. The functionalized single walled carbon nanotubes may then may further heated or or the adsorbed molecules may be subjected to partial pyrolysis to prevent desorption. Other mechanisms for anchoring the adsorbed molecule such as crosslinking or oligomerization (to decrease solubility) may be used.
  • Prefered planar aromatic compounds for adsorption include porphyrins and phthalocyanines,
  • the adsorbed cyclic compounds may be functionalized.
  • Such compositions include compounds of the formula
  • m, n, L, a, X and A are as defined above and the carbons are surface carbons of a substantially cylindrical graphitic or single walled carbon nanotube as described above.
  • the carbon fibrils functionalized as described above may be incorporated in a matrix.
  • the matrix is an organic polymer (e.g., a thermoset resin such as epoxy, bismaleimide, polyamide, or polyester resin; a thermoplastic resin; a reaction injection molded resin; or an elastomer such as natural rubber, styrene-butadiene rubber, or cis-1,4- polybutadiene); an inorganic polymer (e.g., a polymeric inorganic oxide such as glass), a metal (e.g., lead or copper), or a ceramic material (e.g., Portland cement).
  • Beads may be formed from the matrix into which the fibrils have been incorporated. Alternately, functionalized fibrils can be attached to the outer surface of functionalized beads.
  • the functionalized fibrils are better dispersed into polymer systems because the modified surface properties are more compatible with the polymer, or, because the modified functional groups (particularly hydroxyl or amine groups) are bonded directly to the polymer as terminal groups.
  • polymer systems such as polycarbonates, polyurethanes, polyesters or polyamides/imides bond directly to the fibrils making the fibrils easier to disperse with improved adherence.
  • the invention is also in methods of introducing functional groups onto the surface of carbon fibrils by contacting carbon fibrils with a strong oxidizing agent for a period of time sufficient to oxidize the surface of said fibrils and further contacting said fibrils with a reactant suitable for adding a functional group to the oxidized surface.
  • the oxidizing agent is comprised of a solution of an alkali metal chlorate in a strong acid.
  • the alkali metal chlorate is sodium chlorate or potassium chlorate.
  • the strong acid used is sulfuric acid. Periods of time sufficient for oxidation are from about 0.5 hours to about 24 hours.
  • a composition having the formula [C ⁇ H L ⁇ fCH(R')OH] m , wherein n, L, R' and m are as defined above, is formed by reacting R'CHbOH with the surface carbons of a nanotube in the presence of a free radical initiator Attorney DTOet No. 100647-03591
  • the invention is also in a method for linking proteins to nanotubes modified by an NHS ester, by forming a covalent bond between the NHS ester and the amino group of the protein.
  • the invention is also in methods for producing a network of carbon fibrils or single walled carbon nanotubes comprising contacting carbon fibrils or single walled carbon nanotubes with an oxidizing agent for a period of time sufficient to oxidize the surface of the carbon fibrils or single walled carbon nanotubes, contacting the surface-oxidized carbon fibrils or single walled carbon nanotubes with reactant suitable for adding a functional group to the surface of the carbon fibrils or single walled carbon nanotubes, and further contacting the surface-functionalized fibrils with a cross-linking agent effective for producing a network of carbon fibrils or single walled carbon nanotubes.
  • a preferred cross-linking agent is a polyol, polyamine or polycarboxylic acid.
  • Functionalized fibrils or single walled carbon nanotubes also are useful for preparing rigid networks of fibrils or networks of single walled carbon nanotubes.
  • a well- dispersed, three-dimensional network of acid-ftinctionalized fibrils or single walled carbon nanotubes may, for example, be stabilized by cross-linking the acid groups (inter-fibril) with polyols or polyamines to form a rigid network.
  • the invention also includes three-dimensional networks formed by linking ninctionalized fibrils or single walled carbon nanotubes of the invention.
  • These complexes include at least two functionalized fibrils or single walled carbon nanotubes linked by one or more linkers comprising a direct bond or chemical moiety.
  • These networks comprise porous media of remarkably uniform equivalent pore size. They are useful as adsorbents, catalyst supports and separation media.
  • interstices between these fibrils or single walled carbon nanotubes are irregular in both size and shape, they can be thought of as pores and characterized by the methods used to characterize porous media.
  • the size of the interstices in such networks can be controlled by the concentration and level of dispersion of fibrils, and the concentration and chain lengths of the cross-linking agents.
  • Such materials can act as structured catalyst supports and may be tailored to exclude or include molecules of a certain size. Aside from conventional industrial catalysis, they have special applications as large pore supports for biocatalysts.
  • the rigid networks can also serve as the backbone in biomimetic systems for molecular recognition. Such systems have been described in U.S. Patent No. 5,110,833 and Attorney Docket No. 100647-03591 16
  • the uniformly functionalized fibrils of the invention can be directly prepared by sulfonation, electrophilic addition to deoxygenated fibril surfaces or metallation.
  • arc grown nanofibers When arc grown nanofibers are used, they may require extensive purification prior to functionalization. Ebbesen et al. (Nature 367 519 (1994)) give a procedure for such purification.
  • the carbon fibrils are processed prior to contacting them with the functionalizing agent.
  • processing may include dispersing the fibrils in a solvent.
  • the carbon fibrils may then be filtered and dried prior to further contact.
  • Activated C-H (including aromatic C-H) bonds can be sulfonated using fuming sulfuric acid (oleum), which is a solution of cone, sulfuric acid containing up to 20% SO3.
  • oleum fuming sulfuric acid
  • the conventional method is via liquid phase at T-80°C using oleum; however, activated C-H bonds can also be sulfonated using SO 3 in inert, aprotic solvents, or SO 3 in the vapor phase.
  • the reaction is:
  • the SO3 source was connected to the reactor tube and an argon stream was used to carry SO 3 vapors into the quartz tube reactor. Reaction was carried out for the desired time at the desired temperature, after which the reactor was cooled under flowing argon. The fibrils were then dried at 90°C at 5" Hg vacuum to obtain the dry weight gain. Sulfonic acid (-SO 3 H) content was determined by reaction with 0.10ON NaOH and back-titration with 0.10ON HCl using pH 6.0 as the end point.
  • the surface carbons in fibrils behave like graphite, i.e., they are arranged in Attorney D3Hcet No. 100647-03591 18 hexagonal sheets containing both basal plane and edge carbons. While basal plane carbons are relatively inert to chemical attack, edge carbons are reactive and must contain some heteroatom or group to satisfy carbon valency. Fibrils also have surface defect sites which are basically edge carbons and contain heteroatoms or groups.
  • Fibril-O Reactive Fibril Surface (RFS) + 2 CO + CO 2 followed by:
  • R' is a hydrocarbon radical (alkyl, cycloalkyl, etc.)
  • KL3 2423199 1 Attorney D ⁇ cet No. 100647-03591 19 tube fitted with a thermocouple and situated in a Lindberg tube furnace. The ends are fitted with a gas inlet/outlets. The tube is purged with dry, deoxygenated argon for 10 minutes, after which the temperature of the furnace is raised to 300°C and held for 30 minutes. Thereafter, under a continued flow of argon, the temperature is raised in 100 0 C increments to 1000 0 C, and held there for 16 hours. At the end of that time, the tube is cooled to room temperature (RT) under flowing argon.
  • RT room temperature
  • the flow of argon is then shunted to pass through a multi-neck flask containing neat purified acrylic acid at 50 0 C and fitted with gas inlet/outlets.
  • the flow of acrylic acid/argon vapors is continued at RT for 6 hours.
  • residual unreacted acrylic acid is removed, first by purging with argon, then by vacuum drying at 100 0 C at ⁇ 5" vacuum.
  • the carboxylic acid content is determined by reaction with excess 0,10ON NaOH and back-titrating with 0.100N HCL to an endpoint at pH 7.5.
  • Aromatic C-H bonds can be metallated with a variety of organometallic reagents to produce carbon-metal bonds (C-M).
  • M is usually Li, Be, Mg, Al, or Tl; however, other metals can also be used.
  • the simplest reaction is by direct displacement of hydrogen in activated aromatics:
  • the reaction may require additionally, a strong base, such as potassium t-butoxide or chelating diamines.
  • a strong base such as potassium t-butoxide or chelating diamines.
  • Aprotic solvents are necessary (paraffins, benzene).
  • the metallated derivatives are examples of primary singly-functionalized fibrils. However, they can be reacted further to give other primary singly-functionalized fibrils. Some reactions can be carried out sequentially in the same apparatus without isolation of intermediates.
  • Fibril-M + X 2 > Fibril-X + MX X Halogen catalyst Fibril-M + CH 3 ONH 2 .HC1 > Fibril-NH 2 + MOCH 3 ether
  • CC fibrils are placed in a porcelain boat and inserted into a 1" quartz tube reactor which is enclosed in a Lindberg tube furnace. The ends of the tube are fitted with gas inlet/outlets. Under continuous flow of H 2 , the fibrils are heated to 700 0 C for 2 hours to convert any surface oxygenates to C-H bonds. The reactor is then cooled to RT under flowing H 2 .
  • Fibrils are transferred to a 50 cc r.b. flask fitted with a stopcock and dried under 10 "4 torr vacuum at 5O 0 C.
  • the lithium concentration is determined by reaction of a sample of fibrils with excess 0.10ON HCl in DI water and back-titration with 0.100N NaOH to an endpoint at pH 5.0.
  • One gram of thallated fibrils is prepared as in Ex. 7.
  • the fibrils are slurried in dioxane and 0.5 g triphenyl phosphine dissolved in dioxane is added.
  • the slurry is stirred at 50°C for several minutes, followed by addition at 50 0 C of gaseous ammonia for 30 min.
  • the fibrils are then separated by filtration, washed in dioxane, then DI water and dried at 80°C at 5" vacuum.
  • the amine concentration is determined by reaction with excess acetic anhydride and back-titration of free acetic acid and unreacted anhydride with 0.10ON NaOH.
  • the graphitic surfaces of fibrils allow for physical adsorption of aromatic compounds.
  • the attraction is through van der Waals forces. These forces are considerable between multi-ring heteronuclear aromatic compounds and the basal plane carbons of graphitic surfaces. Desorption may occur under conditions where competitive surface adsorption is possible or where the adsorbate has high solubility.
  • fibrils can be functionalized by the adsorption of phthalocyanine derivatives. These phthalocyanine derivative fibrils can then be used as solid supports for protein immobilization. Different chemical groups can be introduced on the fibril surface simply by choosing different derivatives of phthalocyanine.
  • phthalocyanine derivative fibrils for protein immobilization has significant advantages over the prior art methods of protein immobilization. In particular, it is simpler than covalent modifications. In addition, the phthalocyanine derivative fibrils have high surface area and are stable in almost any kind of solvent over a wide range of temperature and pH.
  • the preferred compounds for physical adsorption on fibrils are derivatized porphyrins or phthalocyanines which are known to adsorb strongly on graphite or carbon blacks.
  • Several compounds are available, e.g., a tetracarboxylic acid porphyrin, cobalt (II) phthalocyanine or dilithium phthalocyanine. The latter two can be derivatized to a carboxylic acid form.
  • the two Li + ions are displaced from the phthalocyanine (Pc) group by most metal (particularly multi-valent) complexes. Therefore, displacement of the Li + ions with a metal ion bonded with non-labile ligands is a method of putting stable functional groups onto fibril surfaces. Nearly all transition metal complexes will displace Li + from Pc to form a stable, non-labile chelate. The point is then to couple this metal with a suitable ligand.
  • Cobalt (II) complexes are particularly suited for this.
  • Co 4+ ion can be substituted for the two Li + ions to form a very stable chelate.
  • the Co + * ion can then be coordinated to a ligand such as nicotinic acid, which contains a pyridine ring with a pendant carboxylic acid group and which is known to bond preferentially to the pyridine group.
  • a ligand such as nicotinic acid, which contains a pyridine ring with a pendant carboxylic acid group and which is known to bond preferentially to the pyridine group.
  • Co(II)Pc can be electrochemically oxidized to
  • Suitable ligands are the aminopyridines or ethylenediamine (pendant
  • the loading capacity of the porphyrin or phthalocyanines can be determined by decoloration of solutions when they are added incrementally.
  • the deep colors of the solutions deep pink for the tetracarboxylic acid porphyrin in MeOH, dark blue-green for the
  • Co(II) or the dilithium phthalocyanine in acetone or pyridine are discharged as the molecules are removed by adsorption onto the black surface of the fibrils.
  • Loading capacities were estimated by this method and the footprints of the derivatives were calculated from their approximate measurements ( ⁇ 140 sq. Angstroms).
  • maximum loading will be -0.3 mmol/g.
  • the tetracarboxylic acid porphyrin was analyzed by titration. The integrity of the adsorption was tested by color release in aqueous systems at ambient and elevated temperatures.
  • the fibril slurries were initially mixed (Waring blender) and stirred during loading. Some of the slurries were ultra-sounded after color was no longer discharged, but with no effect.
  • a number of substituted polynuclear aromatic or polyheteronuclear aromatic compounds were adsorbed on fibril surfaces.
  • the number of aromatic rings should be greater than two per rings/pendant functional group.
  • substituted anthracenes, phenanthrenes, etc. containing three fused rings, or polyfunctional derivatives containing four or more fused rings can be used in place of the porphyrin or phthalocyanine derivatives.
  • substituted aromatic heterocycles such as the quinolines, or multiply substituted heteroaromatics containing four or more rings can be used.
  • Table II summarizes the results of the loading experiments for the three porphyrin/phthalocyanine derivatives.
  • CoPhth Cobalt(II) Phthalocyanine
  • thermolysin on these fibrils was determined by measuring the enzyme activity of the fibrils.
  • Thermolysin can react with substrate FAGLA (N-(3-[2- furyl]acryloyl)-gly-leuamide) and produce a compound that causes absorbance decrease at 345 nm with extinction coefficient of -310 M 1 Cm "1 .
  • the assay buffer condition for this reaction was 4OmM Tris, 1OmM CaCl 2 and 1.75 M NaCl at pH 7.5.
  • the reaction was performed in 1 ml cuvette by mixing 5 ⁇ l of FAGLA stock solution (25.5 mM in 30% DMF Attorney D3BIcet No.
  • thermolysin fibrils 100647-03591 26 in CiH 2 O) and lO ⁇ g of thermolysin fibrils in 1 ml of assay buffer.
  • the absorbance decrease at 345 nm was monitored by time scan over 10 minutes.
  • the enzyme activity ( ⁇ M/min) was then calculated from the initial slope using the extinction coefficient -310 M -1 Cm "1 .
  • the amount of active thermolysin per gram of fibril was 0.61 ⁇ moles.
  • Thermolysin was immobilized on these phthalocyanine derivative fibrils by adsorption according to the method of Example 34.
  • the amount of active thermolysin per gram of fibrils was 0.70 ⁇ moles.
  • Phthalocyanine derivative fibrils on which thermolysin has been immobilized can be used to catalyze the synthesis of a precursor of the artificial sweetener aspartame.
  • the reaction is carried out by mixing 80 mM L-Z-Asp and 220 niM L-PheOMe in ethyl acetate with 10 ⁇ M fibril immobilized thermolysin.
  • the product Z-Asp-PheOMe is monitored by HPLC to determine the yield.
  • a weighed sample of fibrils was slurried with nitric acid of the appropriate strength in a round bottom multi-neck indented reactor flask equipped with an overhead stirrer and a water condenser. With constant stirring, the temperature was adjusted and the reaction carried out for the specified time. Brown fumes were liberated shortly after the temperature exceeded 70 0 C, regardless of acid strength. After the reaction, the slurry was poured onto cracked ice and diluted with DI water. The slurry was filtered and excess acid removed by washing in a Soxhlet extractor, replacing the reservoir with fresh DI water every several hours, until a slurried sample gave no change in Ph from DI water. The fibrils were dried at 100 0 C at 5" vacuum overnight.
  • Amino groups can be introduced directly onto graphitic fibrils by treating the fibrils with nitric acid and sulfuric acid to get nitrated fibrils, then reducing the nitrated form with a reducing agent such as sodium dithionite to get amino-functionalized fibrils according to the following formula:
  • the resulting fibrils have many utilities, including the immobilization of proteins (e.g., enzymes and antibodies), and affinity and ion exchange chromatography.
  • proteins e.g., enzymes and antibodies
  • affinity and ion exchange chromatography e.g., affinity and ion exchange chromatography
  • the reaction mixture is filtered and the carbon nanotube material is washed and dried, yielding modified nanotubes of the formula Nanotube-CH(R)OH.
  • This method can also be used to couple bifunctional alcohols. This allows one end to be linked to the carbon nanotube and the other to be used for the indirect linkage of another material to the surface.
  • Non-specific binding to high surface area carbon material is ubiquitous. It has been found that attaching hydrophilic oligomers such as PEG to carbon nanotubes can reduce non-specific binding. Further, it has been found that by attaching one end of chain- like molecules such as PEG to the surface of the nanotubes the free end can contain a functional group that can be used for attachment of other materials of interest while still retaining the properties of the PEG (or other material) layer to reduce non-specific binding. Reduction of Non-specific Binding of Bovine Serum Albumen with PEG-modified Fibrils
  • R alkyl, aralkyl, aryl, R- Methanol, phenol, tri- fluoroethanol, polymer, SiR'3 fluorocarbon, OH-terminated
  • H 2 N-R R same as above R- Amines, anilines, fluorinated amines, silylamines, amine terminated polyamides, proteins
  • HO-R-OH, R alkyl, HO- Ethyleneglycol, PEG, Penta- aralkyl, CH 2 O- erythritol, bis-Phenol A
  • H 2 N- Ethylenediamine polyethyl- aralkyl eneamines
  • the reactions can be carried out using any of the methods developed for esterifying or aminating carboxylic acids with alcohols or amines.
  • the methods of H.A. Staab, Anagew. Chem. Intemat. Edit., (1), 351 (1962) using N,N'-carbonyl diimidazole (CDI) as the acylating agent for esters or amides and of G. W. Anderson, et al., J. Amer. Chem. Soc. 86, 1839 (1964), using N-hydroxysuccinimide (NHS) to activate carboxylic acids for amidation were used.
  • CDI N,N'-carbonyl diimidazole
  • NHS N-hydroxysuccinimide
  • DABCO Diaza- 1,1,1 -bicyclooctane
  • Suitable solvents are dioxane and toluene.
  • Aryl sulfonic acids as prepared in Example 1, can be further reacted to yield secondary derivatives.
  • Sulfonic acids can be reduced to mercaptans by L1AIH 4 or the combination of triphenyl phosphine and iodine (March, J.P., p. 1107). They can also be converted to sulfonate esters by reaction with dialkyl ethers, i.e., Fibril ⁇ SO 3 H + R-O-R
  • This method is particularly useful for the covalent attachment of protein to graphitic fibrils via the free NH 2 on the protein's side chain.
  • proteins which can be immobilized on fibrils by this method include trypsin, streptavidin and avidin.
  • streptavidin (or avidin) fibrils provide a solid carrier for any biotinylated substance.
  • streptavidin fibrils were stored in PBS buffer for further use.
  • Trypsin fibrils were prepared by mixing 1.1 mg NHS-ester fibrils (treated as in avidin fibrils) and 200 ⁇ l of 1.06 mM trypsin solution made in 5 mM sodium phosphate buffer (pH 7.1) and rotating at room temperature for 6.5 hours. The trypsin fibrils were then washed by 1 ml of 5 mM sodium phosphate buffer (pH 7.1) three times and suspended in 400 ⁇ l of the same buffer for storage.
  • Trypsin can react with substrate L-BAPNA (N ⁇ -benzoyl-L-arginine p- nitroanilide) and release a colored compound that absorbs light at 410 nm.
  • the assay buffer for this reaction was 0.05 M Tris, 0.02 M CaCl 2 , pH 8.2.
  • the reaction was performed in 1 ml cuvette by mixing 5 ⁇ l of L-BAPNA stock solution (50 mM in 37% DMSO in H 2 O) and 10-25 ⁇ g of trypsin fibrils in a 1 ml of assay buffer.
  • the absorbance increase at 410 nm was monitored over 10 minutes.
  • the enzyme activity ( ⁇ M/min) was then calculated from the initial slope.
  • the activity was 5.24 ⁇ M/min per 13 ⁇ g fibrils. This result can be converted to the amount of active trypsin on fibrils by dividing the activity of a known concentration of trypsin solution, which was measured to be 46 ⁇ M/min per 1 ⁇ M trypsin under the same assay conditions. Therefore the amount of active trypsin per gram of fibrils was 8.3 ⁇ moles (or 195 mg).
  • a 10 mg sample of thiolated nanotubes was suspended in 10 mis. of DI water with sonication and filtered onto 0.45 ⁇ m nylon membrane to form a felt-like mat.
  • the mat section was stored in a vacuum desiccator prior to analysis by ESCA which showed 0.46% sulfur and 1.69% nitrogen, confirming successful conversion to thiol-modified CN.
  • Amino fibrils were prepared according to Example 13. The amino fibrils
  • maleimides with different linkers e.g., sulfo-SMCC, succinimidyl 4-[p-maleimidophenyl]butyrate [SMPB], sulfo- SMPB, m-maleimidobenzyl-N-hydroxysuccinimide ester [MBS], sulfo-MBS etc.
  • linkers e.g., succinimidyl 4-[p-maleimidophenyl]butyrate [SMPB], sulfo- SMPB, m-maleimidobenzyl-N-hydroxysuccinimide ester [MBS], sulfo-MBS etc.
  • the resulting maleimide fibrils can be used as a solid support for the covalent immobilization of proteins, e.g., antibodies and enzymes, Antibodies were covalently immobilized on malemide activated fibrils.
  • the capacity of antibody was 1.84 milligrams per gram of fibrils when amino fibrils obtained from nitration/reduction method (Example 13) were used and 0.875 milligrams per gram of fibrils when amino fibrils derivatized from carboxyl fibrils were used.
  • the carboxylic acid content was 0.75 meq/g.
  • Fibrils were reacted with a stoichiometric amount of CDI in an inert atmosphere with toluene as solvent at R.T. until CO2 evolution ceased. Thereafter, the slurry was reacted at 80 0 C with a 10-fold molar excess of polyethyleneglycol (MW 600) and a small amount of NaOEt as catalyst. After two hours reaction, the fibrils were separated by filtration, washed with toluene and dried at 100 0 C.
  • ESCA was carried out to quantify the amount of N present on the aminated fibrils (GFZNH 2 ).
  • ESCA analysis of 177-046-1 showed 0.90 at% N (177-059).
  • a derivative was made by the gas phase reaction with pentafluorobenzaldehyde to produce the corresponding Schiff Base linkages with available primary amine groups.
  • ESCA analysis still showed the 0.91 at% N, as expected, and 1.68 at%F. This translates into a 0.34 at% of N present as reactive primary amine on the aminated fibrils (5 F per pentafluorobenzaldehyde molecule).
  • a level of 0.45 at% N would be expected assuming complete reaction with the free ends of each N. The observed level indicates a very high yield from the reaction of N with NHS-activated fibril and confirms the reactivity of the available free amine groups.
  • 1,6-diaminohexane (a six-carbon linker), rather than ethylenediamine (a two-carbon linker).
  • Carboxyl groups on fibrils can be modified by reacting the carboxyl groups with one amino group of a compound having two or more amino groups (at least one of which is unprotected by groups such as t-Boc or CBZ).
  • the fibrils so generated are amide Attorney lWkct No. 100647-03591 38 derivatives in which the amide carbonyl is derived from the fibril carboxyl group and the amide nitrogen is substituted with a group (such as an alkyl group) containing one or more primary amines.
  • the amino groups are then available for use or further modification.
  • N-boc-l,6-diaminohexane hydrochloride (1.94 g, 7.7 mmol) was partitioned between dichloromethane (10 mL) and 1 M NaOH (10 mL). The lower, organic phase was dried over anhydrous potassium carbonate and filtered through a disposable Pasteur pipette containing a cotton plug, and N-methylmorpholine (758 ⁇ L, 7 mmol) was added.
  • Acid functionalized fibrils prepared as in Example 14 were slurried in dioxane in an inert atmosphere. With stirring, a stoichiometric amount of chlorotriethyl silane was added and reacted for 0.5 hr, after which several drops of a 5% solution of DABCO in dioxane was added. The system was reacted for an additional hour, after which the fibrils were collected by filtration and washed in dioxane. The fibrils were dried at 100 0 C in 5" vacuum overnight.
  • Table 5 summarizes the secondary derivative preparations. The products were analyzed by ESCA for C, O, N, Si and F surface contents.
  • Acid functionalized fibrils prepared as in Example 14 are slurried in dioxane in an inert atmosphere. With stirring, a stoichiometric amount of chlorotriethyl silane is added and reacted for 0.5 hr, after which several drops of a 5% solution of DABCO in dioxane is added. The system is reacted for an additional hour, after which the fibrils are collected by filtration and washed in dioxane. The fibrils are dried at 100 0 C in 5" vacuum overnight.
  • Table VI summarizes the secondary derivative preparations. Products are analyzed by ESCA. The analysis confirms the incorporation of the desired pendant groups. The products are analyzed by ESCA for C, O, N, Si and F surface contents. Attorney D ⁇ Met No. 100647-03591 40
  • Tertiary and quaternary amine functional groups can be attached to the surface of carbon nanotubes via an amide or ester bond via a carboxyl group on the nanotube and either an amine or hydroxyl group of the tertiary or quaternary amine precursor.
  • Such tertiary or quaternary amine fibrils are useful as chromatographic matrices for the separation of biomolecules.
  • the tertiary or quaternary amine fibrils can be fabricated into disk-shaped mats or mixed with conventional chromatographic media (such as agarose) for separation purposes.
  • the resulting fibrils were washed three times with 20 ml dimethylformamide, three times with 20 ml methylene chloride, three times with 20 ml methanol and finally three times with de-ionized water.
  • the product was dried under vacuum. Results from an elemental analysis of nitrogen showed that about 50% of the carboxyl groups on the fibril had reacted with the primary amino group in the quaternary amine moiety.
  • BSA Serum Albumin
  • the column was eluted with 5 mM sodium phosphate at a flow rate of 0.2 ml/min and 0.6 ml fractions were collected.
  • the elution profile was monitored using a UV- visible detector, and is shown in Fig 3. Once the detector indicated that no more protein was eluting from the column, bound BSA was eluted by adding 1 M KCl in 5 mM sodium phosphate (pH 7.3). The presence of the protein in each fraction was identified by micro BCA assay (Pierce, Rockford, II).
  • the elution profile was monitored using a UV-visible detector (Fig. 4). Once the detector indicated that protein was no longer being eluted with 5 mM sodium phosphate buffer, the solvent was changed to 1 M KCl in 5 mM sodium phosphate (pH 7.3). The presence of the protein in each fraction was identified by micro BCA assay (Pierce, Rockford, II). Attorney DMet No. 100647-03591 42
  • Biocatalysts can be used to introduce functional groups onto the surface of graphitic carbon, especially carbon nanotubes.
  • graphitic carbon has been modified by purely chemical means (see e.g., U.S. Application Serial No. 08/352,400, filed December 8, 1994). These chemical methods have drawbacks of: (1) harshness of conditions (use of extreme temperatures, extreme acidity or toxic chemicals), and (2) lack of specificity (e.g., oxidation can introduce COOH, COH, and CHO groups).
  • Aqueous suspensions of solid graphitic carbon are made containing one or more enzymes that are capable of accepting the graphitic carbon as a substrate and performing a chemical reaction resulting in chemically-modified graphitic carbon.
  • the aqueous suspension is maintained at conditions acceptable for the enzyme(s) to carry out the reaction (temperature, pH, salt concentration, etc.) for a time sufficient for the enzyme(s) to catalytically modify the surface of the graphitic carbon.
  • the suspension is continually mixed to allow the enzyme(s) access to the surface of the graphitic carbon.
  • the enzyme is removed from the carbon by filtration washing.
  • cytochrome p450 enzymes and peroxidase enzymes.
  • the types of enzymes have been well-studied, they accept aromatic type substrates, and their optimal reaction conditions have been worked out. Both enzyme types introduce hydroxyl groups into their substrates and may introduce hydroxyl groups into graphitic carbon.
  • biocatalysts such as ribozymes and catalytic antibodies, or non-biological mimics of enzymes, could be designed to catalytically functionalize carbon nanotubes.
  • Cytochrome p450 enzymes are generally believed to function in the liver as detoxifying agents (F. Peter Guengerich, American Scientist, 81, 440-447 and F. Peter Guengerich, J. Biol. Chem., 266, 10019-10022). They hydroxylate foreign compounds such as polyaromatic toxic compounds. Hydroxylation allows these compounds to become water soluble so that they can be eliminated from the body via the urine.
  • cytochrome p450 enzymes in the liver each with different substrate specificities. These broad range of specificities is believed to be important because of the wide range of environmental toxins whose detoxification is required. Although individual cytochrome p450s are commercially available, no information is available regarding whether any of
  • KL3:2423I99.1 Attorney D ⁇ Met No. 100647-03591 43 these would accept carbon nanotubes as a substrate. Because of this uncertainty, we decided to initially incubate carbon nanotubes with a rat liver extract which contained many different cytochrome p450s.
  • cytochrome p450 enzymes Two other rats (“control" rats) were given water without phenobarbital. The rats were then sacrificed and cytochrome p450-containing microsomes were prepared from their livers by standard procedures (see for example, Methods in Enzymology, Vol. 206). [00186] The microsomes were mixed with carbon nanotubes (fibrils) to allow the cytochrome p450s to react with the graphitic carbon.
  • fibrils both "plain” or nonfunctionalized and “COOH” or oxidized fibrils
  • microsomes both experimental and control microsomes
  • 0.1 M Tris 1.0 mM NADPH, 0.01% NaN 3 , 10 mM glucose-6-phosphate, glucose-6- phosphate dehydrogenase (1 unit/mL), pH 7.4.
  • NADPH was included as a co-substrate for cytochrome p450s and glucose-6-phosphate, glucose- 6-phosphate dehydrogenase were added to regenerate NADPH from NADP + (if NADP + is generated by cytochrome p450s).
  • the mixtures were rotated at room temperature for about 1.5 days in microcentrifuge tubes. Following the incubation, the fibrils were washed extensively in deionized water, 1 M HCl, 1 M NaOH, 0.05% Triton X-100, 0.05% Tween, methanol, and 1 M NaCl. Following washing, microBCA assay for proteins (Pierce) showed that fibrils seemed to still have protein associated with them (although no protein was detected in the wash solution). [00187] To determine whether hydroxyl groups had been introduced onto the fibril surfaces, the fibrils were reacted with N-FMOC-isoleucine.
  • cytochrome p450 enzymes were purchased (GENTEST, Woburn, MA). Because cytochrome p450 enzymes are only active in association with membranes, these enzymes are supplied as microsomal preparations. Using a reaction procedure similar to that described above, we tested the following cytochrome p450s: CYPlAl (cat.# MlUb), CYP1A2 (cat.# M103c), CYP2B6 (cat.# HOa), CYP3A4 (with reductase, cat J 107r).
  • MgCh (0.67 mg/mL) was also included in the reaction solution.
  • fibrils were washed with the aid of a Soxhlet apparatus.
  • Analysis of introduced hydroxyl groups was carried out by reaction of cytochrome p450-reacted, washed fibrils with the colored reagent 3,5-dinitrobenzoic acid (DNBA). Coupling was carried out as described above for N-FMOC-isoleucine. Following reaction with DNBA, the fibrils were washed with DMF and residual (covalently attached) DNBA was hydro lyzed using either 6 M HCl or 46 units/mL pig liver esterase (Sigma).
  • HPLC analysis of liberated DNBA was carried out by HPLC analysis of the supernatant surrounding the fibrils following hydro lytic treatment.
  • HPLC analysis of liberated DNBA was carried out on a Waters HPLC system equipped with a Vydac Cl 8 reversed phase analytical column (cat.# 218TP54) and a linear gradient from deionized water containing 0.1% TFA (solvent A) to acetonitrile containing 0.1% TFA (solvent B).
  • fibrils 11 mg were mixed in a solution containing 50 mM sodium acetate (1.25 mL, pH 5.0), horseradish peroxidase (200 nM), and dihydroxyfumaric acid (15 mg) was added 5 mg at a time for the first 3 hours of the reaction. The reaction was carried out for a total of 5
  • the concentration of functional groups on the surface of nanotubes can be increased by modifying the nanotubes with a series of generations of a polyfunctional reagent that results in the number of the specific functional groups increasing with each generation to form a dendrimer-like structure.
  • the resulting dendrimeric nanotubes are particularly useful as a solid support upon which to covalently immobilize proteins, because they increase the density of protein immobilized on the nanotube surface.
  • the present invention demonstrates that high densities of a specific chemical functionality can be imparted to the surface of high surface area particulate carbon, which has been difficult with previous high surface area carbons
  • the product amino lysine fibrils were extensively washed with methylene chloride, methanol and water and dried under vacuum. Preparation of the second and the third generation lysine fibrils followed the same procedure.
  • the amino acid analysis data showed that the first generation lysine fibrils contained 0.6 ⁇ mols lysine per gram of fibrils, the second generation lysine fibrils contained 1.8 ⁇ mols per gram of fibrils, and the third generation lysine had 3.6 ⁇ mols lysine per gram of fibrils.
  • Carboxyl dendrimeric fibrils can be prepared by the same method by using aspartic or glutamic acid with carboxyl fibrils.
  • Carboxylate terminated dendrimers with a carbon nanotube (CN) core are produced by successive, sequential couplings of aminobuty-nitrilotriacetic acid (NTA) and Attorney D ⁇ Ket No. 100647-03591 47 beginning with the NHS ester of chlorate oxidized carbon nanotubes. Preparation of NTA
  • NTA was prepared according to the method of Hochuli (E. Hochuli, H.
  • CN/NTA was first converted to the NHS active ester. 0.396 grams of
  • CN/NTA was dried in an oven at 90 0 C for 30 minutes and then placed in a 100 ml RB flask with 30 mis of anhydrous dioxane and purged with argon.
  • 0.4 g of N-hydroxysuccinimide added with stirring followed by 0.67 grams of EDC with continued stirring for an additional hour.
  • the CN tended to agglomerate together during this time.
  • the dioxane was decanted off and the solids were washed 2X with 20 mis of anhydrous dioxane.
  • the solids were washed with 20 mis of anhydrous MeOH during which the agglomerates broke up.
  • the solids were filtered onto a 0.45 ⁇ m nylon membrane, resuspended in MeOH, filtered and washed on the filter with MeOH.
  • HRP horseradish peroxidase
  • second generation lysine fibrils and third generation lysine fibrils were sonicated with sodium bicarbonate conjugate buffer (600 ⁇ l, 0.1 M, containing 0.9% NaCl) for 15 minutes at room temperature. Then they were incubated with HRP solution in sodium bicarbonate conjugate buffer (490 ml, enzyme stock solution of 5.6 mg/ml) for 19 hours at room, temperature.
  • the HRP immobilized fibrils were washed with the following buffer (1 ml): 10 mM NaHCO 3 buffer containing 0.9% NaCl at pH 9.5 (IX washing buffer) seven times, 0.1% Triton X-100 in IX washing buffer five times, 50% ethylene glycol in IX washing buffer three times.
  • a functional group e.g., a carboxyl group and an amino group
  • a functionalized nanotube e.g., a carboxy nanotube
  • Such bifunctional fibrils can be used to immobilize multiple molecules, particularly in 1: 1 stoichiometrics and in close proximity.
  • N ⁇ -CBZ-N ⁇ -(tert- butoxycarbonyl)-L-lysine was treated with 0.2 M calcium carbonate (4 ml) and the aqueous layer was removed to obtain a white solid.
  • the solid was resuspended in N,N-dimethylformamide (40 ml) and benzyl bromide (1.16 ml). The reaction mixture was stirred overnight at room temperature. The reaction mixture was worked up with ethyl acetate and water, and the organic layer was dried over magnesium sulphate.
  • N ⁇ -CBZ-L-lysine benzyl ester fibrils (113 mg) in methanol (4 ml) was added sodium hydroxide (1 N, 4 ml) and the reaction mixture was stirred overnight.
  • the product N ⁇ -CBZ-L-lysine fibrils was extensively washed with water and methanol and the fibrils were dried under vacuum.
  • To a suspension of N ⁇ -CBZ-L-lysine fibrils (50 mg) in acetonitrile (4 ml) was added trimethyl silyl iodide (1 ml). The mixture was stirred for 3 hours at 4O 0 C.
  • the final bifunctional fibrils were extensively washed with water, methanol, 0.5 N sodium hydroxide, acetonitrile and methylene chloride. Amino acid analysis showed 0.3 ⁇ mols lysine per gram of fibrils.
  • Hydroxyl and carboxyl (or amino) bifunctional fibrils can be made by a similar method to that described here by using serine, threonine, or tyrosine.
  • Thiolated and carboxyl (or amino) bifunctional fibrils can be made using cysteine.
  • Carboxyl and amino bifunctional fibrils can be made using aspartic or glutamic acid.
  • Functionalized graphitic nanotubes are useful as solid supports in many biotechnology applications due to their high porosity, chemical and thermal stability and high surface area. They have been found to be compatible with harsh chemical and thermal treatments and very amenable to chemical functionalization.
  • an enzyme can be covalently immobilized on a modified nanotube while retaining its biological activity.
  • nanotubes are also suitable for use as affinity chromatographic supports in biomolecular separations.
  • enzyme inhibitors have been prepared on nanotubes in multi-step syntheses such that the immobilized inhibitors were accessible to macromolecules, and reversible specific biological recognition occurred between proteins and modified fibrils.
  • the hydrophobicity of the nanotube surface is not enough to immobilize high densities of proteins by adsorption.
  • alkyl is added to increase the hydrophobicity of the nanotube surface and to expand the hydrophobic environment from two dimensions to three dimensions.
  • KL32423199 1 Attorney D ⁇ 5 ⁇ cet No. 100647-03591 51 chains of varying lengths have been coupled to the nanotube surface.
  • Proteins that have been immobilized on alkyl nanotubes by adsorption include trypsin, alkaline phosphatase, lipase and avidin. The enzyme activities of these immobilized proteins are comparable with those of the free enzymes, proven by the catalytic efficiencies toward the hydrolysis of their substrates in aqueous solutions.
  • phenyl-alkyl nanotubes which are alkyl nanotubes with the addition of a phenyl group on the end of the alkyl chain, have also been prepared.
  • This modification introduced an aromatic structure that interacts with the amino acids phenylalanine, tyrosine, and tryptophan in proteins through ⁇ - ⁇ interactions.
  • the adsorption of alkaline phosphatase and lipase on phenyl-alkyl nanotubes was comparable to the adsorption on Cs-alkyl nanotubes.
  • EDC l-ethyl-3-(3- dimethylaminopropyl)carbodiimide
  • DMAP dimethylaminopyridine
  • Example 41 The lipase fibrils were washed first by dioxane, then a mixture of dioxane and heptane, and finally heptane in order to disperse the fibrils in heptane.
  • ethyl butyrate a food additive which provides pineapple-banana flavor
  • ethanol 0.25M
  • butyric acid 0.25M
  • Phenyl-alkyl fibrils were prepared by two different reactions. Reaction 1 Attorney D ⁇ BEet No. 100647-03591
  • Alkaline phosphatase reacts with substrate p-nitrophenyl phosphate and releases a color compound that absorbs light at 405 nm with extinction coefficient of 18,200 M ⁇ cm "1 .
  • the reaction was performed in 1 ml cuvette by mixing 5 ⁇ l of p- nitrophenyl phosphate stock solution (0.5 M in 33% DMSO in assay buffer) and 13 ⁇ g of alkaline phosphatase fibrils in 1 ml of assay buffer.
  • the absorbance increase of 405 nm was monitored by time scan over 0 minutes.
  • the enzyme activity ( ⁇ M/min) was then calculated from the initial slope using the extinction coefficient 18200 M 4 Cm "1 .
  • the activity was 6.95 ⁇ M/min per 13 ⁇ g fibrils.
  • the activity was 2.58 ⁇ M/min per 13 ⁇ g fibrils.
  • phenyl-alkyl fibrils were suspended in 50 ⁇ l of 5 niM sodium phosphate buffer (pH 7.1) and sonicated for 20 minutes.
  • 5 niM sodium phosphate buffer pH 7.1
  • lipase solution 0.2 mM in 5 mM sodium phosphate buffer, pH 7.1
  • the fibrils were then washed with 600 ⁇ l of 5 mM sodium phosphate buffer (pH 7.1) three times and suspended in 200 ⁇ l of the same buffer.
  • Lipase can react with the substrate l,2-o-dilauryl-rac-glycero-3-glutaric acid- resorufin ester (Boehringer Mannheim, 1179943) and produce a color compound that absorbs light at 572 nm with extinction coefficient of 60,000 M -1 Cm "1 .
  • the reaction was performed in 1 ml cuvette by mixing 5 ⁇ l of substrate stock solution (7.6 mM in 50% dioxane in Thesit) and 13 ⁇ g of alkaline phosphatase fibrils in 1 ml of assay buffer. The absorbance increase at 572 nm was monitored by time scan over 10 minutes. The enzyme activity ( ⁇ M/min) was then calculated from the initial slope using the extinction coefficient 60,000 M "1 cm "1 . [00229] For lipase adsorbed on phenylalkyl fibrils from reaction 1 of Example 43, the activity was 0.078 ⁇ M/min per 13 ⁇ g fibrils.
  • conjugation buffer 0.1 M NaHCO 3 , 0.9% NaCl, pH 9.5
  • conjugation buffer 0.1 M NaHCO 3 , 0.9% NaCl, pH 9.5
  • the fibrils were then washed twice with conjugation buffer in an Eppendorf tube and suspended 430 ⁇ L conjugation buffer.
  • a 50- ⁇ L aliquot of the suspension (0.14 mg fibrils) was mixed with 4.0 mg activated HRP (Pierce, Rockford, IL) dissolved in 50 ⁇ L deionized water and the resulting suspension was rotated overnight at 4°C.
  • the HRP-co ⁇ jugated fibrils were washed extensively in an Eppendorf centrifuge tube with a combination of the following solutions; conjugation buffer, washing buffer (20 mM KH 2 PO 4 , 0.45% NaCl, pH 6.2), washing buffer containing 0.03-0.1% Triton X-100, and washing buffer containing 50% ethylene glycol.
  • conjugation buffer 20 mM KH 2 PO 4 , 0.45% NaCl, pH 6.2
  • washing buffer containing 0.03-0.1% Triton X-100 washing buffer containing 50% ethylene glycol.
  • Immobilized active HRP was quantitated by substrate turnover using H 2 O 2 and the chromogenic substrate 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), diammonium salt (ABTS).
  • Catalytic activity of HRP was spectrophotometrically monitored at 414 nm using 100 ⁇ M H 2 O 2 and 30 ⁇ M ABTS as substrates.
  • the total amount of enzyme bound to amino fibrils in these preliminary studies was 0.0230 ⁇ mol HRP/g fibrils.
  • control (plain fibrils) nonspecifically bound 0.0048 ⁇ mol HRP/g fibrils.
  • the amount of covalently (specifically attached) HRP was 0.0182 ⁇ mol/g fibrils.
  • NHS ester fibrils as described in Example 50 above. NHS ester fibrils (114 mg) were suspended in 4 mL acetone and 10 equivalents (based on the estimation of 0.7 meq NHS ester per gram of fibrils) of tyramine were added. Dry triethylamine (10 equiv.) was added and the mixture was stirred for 3 hours at room temperature. The tyraminyl fibrils were washed under vacuum in a scintered glass funnel first with acetone, then extensively with deionized water.
  • Atomic absorption analysis of arsenic in the AP- inhibitor fibrils was carried out by Galbraith Laboratories (Knoxville, TN). AP-inhibitor fibrils which contain sidechains containing one atom of arsenic were found by atomic absorption analysis to have any arsenic content of 0.4%. This indicates that roughly 10% of the estimated initial COOH groups were converted to AP-inhibitors in this multi-step synthesis. Based on the surface area of fibrils, this means that there would be one inhibitor molecule (enzyme binding site) for every 500A 2 of surface area. Preparation of ⁇ -Galactosidase-Inhibitor Fibrils,
  • TPEG p-Amino-phenyl- ⁇ -D-thiogalactoside
  • PNPP p-nitro-phenylphosphate
  • AP-inhibitor and ⁇ G-inhibitor fibrils For both AP-inhibitor and ⁇ G-inhibitor fibrils, a mixture of AP and ⁇ G were added. To facilitate determinations of specific binding capacities, the concentrations of added enzymes were in large excess of the immobilized inhibitor concentrations. For AP- inhibitor fibrils, 0.550 ⁇ mol AP/g fibrils was bound (as opposed to non-specific binding of 0.020 Amol ⁇ G/g fibrils). For ⁇ G-inhibitor fibrils, the capacity was determined to be 0.093 ⁇ mol ⁇ G/g fibrils (in contrast with non-specific binding of 0.012 ⁇ mol AP/g fibrils). The results of the affinity chromatography experiments are shown in Figs. 9 and 10.
  • AP- inhibitor fibrils did not appreciably bind ⁇ G, but bound AP, which specifically eluted when 40 mM phosphate, a competing inhibitor, was added to the buffer (Fig. 9).
  • Fibrils derivatized with ⁇ G did not bind substantial amounts of AP, but bound ⁇ G, which specifically eluted when the pH was raised to weaken the enzyme-inhibitor association (Fig. 10).
  • antibody nanotubes can be immobilized on fimctionalized nanotubes, and that such antibody nanotubes have unique advantages for many applications due to their high surface area per weight, electrical conductivity, and chemical and physical stability.
  • antibody nanotubes can be used as affinity reagents for molecular separations.
  • Antibody nanotubes are also useful for analytical applications, including diagnostic immunoassays such as ECL-based immunoassays.
  • Antibodies can be immobilized either by covalent binding or non-covalent adsorption. Covalent immobilization was accomplished by various methods; including reductive animation of antibody carbohydrate groups, NHS ester activation of carboxylated fibrils (see Example 27, supra), and reaction of thiolated or maleimido fibrils with reduced or maleimido-modif ⁇ ed antibodies (see Examples 23 and 25 supra). [00241] The best method for attaching antibodies to nanotubes will depend on the application they are to be used in. For separations applications, the preferred method may be non-covalent adsorption because the capacity of protein binding seems to be the highest for this method.
  • NAD + fibrils have been used as a solid support for the purification of dehydrogenases.
  • the main advantage of using fibrils is their large amount of accessible surface area.
  • An affinity matrix with high surface area is desirable because of the high potential capacity.
  • the fibrils may either be a loose dispersion or fixed into a column or mat.
  • Fibrils were oxidized to introduce carboxyl groups according to Examples 14 and 15.
  • sodium bicarbonate solution 3ml, 0.2 M, pH 8.6
  • N 6 -[aminohexyl]carbamoylmethyl)-nicotinamide adenine dinucleotide lithium salt solution 25 mg from Sigma in 5 ml sodium bicarbonate solution.
  • the reaction mixture was stirred overnight at room temperature.
  • the product fibrils were extensively washed with water, N,N-dimethylformarnide, and methanol.
  • the elemental analysis data showed that the product fibrils contained 130 mmols of NAD molecules per gram of fibrils by nitrogen analysis and 147 mmols of NAD molecules per gram of fibrils by phosphorus analysis.
  • Other NAD + analogs having linkers terminating in an amino group can be used to prepare NAD + fibrils.
  • NAD + immobilized fibrils (0.26 mg) and plain fibrils (0.37 mg) were sonicated with 0.1% polyethylene glycol (PEG, MW 1000) in sodium phosphate (1 ml, 0.1 M, at pH 7.1) for 30 minutes at 4O 0 C, then incubated for 30 minutes at 4O 0 C.
  • the fibril suspension was centrifuged and the supernatant were removed.
  • the fibrils were incubated with the mixture of L-lactate dehydrogenase (LDH) in 0.1% PEG (1000) sodium phosphate buffer (250 ⁇ l, the ratio of the LDH solution and the 0.1% PEG buffer was 1 : 1) for 90 minutes at 4 0 C.
  • LDH L-lactate dehydrogenase
  • the assay mixture contained 0.1% PEG (1000) in sodium phosphate buffer (980 ⁇ l), pyruvate (3.3 ⁇ l, 100 mM stock solution), and each elution fraction (16.7 ⁇ l).
  • the enzyme reaction is shown below:
  • control was 3.68 nmols per gram of fibrils.
  • the nonspecific binding of LDH was 5.6%.
  • fibril surfaces can be functionalized by biotinylation or by both alkylation and biotinylation.
  • the fibrils containing such modifications can then bind any streptavidin conjugated substances such as streptavidin beads and streptavidin enzymes.
  • Fibrils offer great advantages as solid carriers because of their high surface area. Beads, which can be made strongly magnetic, are extremely useful in separation assays.
  • the biotinylated fibrils described herein combine the advantages of both the fibrils and the beads.
  • the biotinylated alkyl fibrils are an extension of the same concept but exhibit
  • the streptavidin- and biotin-coated fibrils can be used in diagnostics and can be used as capture agents for assays such as electrocherailuminescence assays.
  • a novel feature of this invention is the combination of two solid carriers on one fibril to create a bifunctional fibril. Moreover, the disclosed process increases the surface area for beads and magnifies fibril magnetization.
  • Biotinylated fibrils were prepared by mixing 2.4 mg of amino fibrils prepared as described in Example 16 and 9 mg of NHS ester long chain biotin in buffer 0.2 M NaHCO3 at a pH of 8.15. The mixture was rotated at room temperature for four hours and washed with the same buffer twice.
  • Biotinylated alkyl fibrils were prepared by a two step reaction. First, 4.25 mg of bifunctional fibrils (containing both amino and carboxyl) and 25 mg of NHS ester long chain biotin were mixed. The fibrils were washed and dried under vacuum. [00253] The second reaction was carried out by mixing 4 mg of biotinylated bifunctional fibrils with 11 mg ofEDC (l-ethyl-3-3-dimethylaminopropyl)carbodiimide), 7.5 mg of DMAP (4-dimethylaminopyridine) and 10 ⁇ l OfNH 2 (CH 2 )VCH 3 in 0.5 ml of DMF. The mixture was stirred at room temperature overnight. The final biotinylated alkyl fibrils were washed by CH 2 Cl 2 , MeOH, and dH 2 O.
  • Biotinylated fibrils can be used in assays involving formats that require streptavidin-biotin or avidin-biotin interactions. Biotinylated fibrils could, for example, be further derivatized with streptavidin. Biotin covalently linked to fibrils (see Example 50) could form strong non-covalent binding interactions with streptavidin. Because streptavidin is a tetrameric protein with four equivalent binding sites, streptavidin bound to biotinylated fibrils would almost certainly have unoccupied binding sites to which additional biotinylated reagents could bind. Thus, biotinylated fibrils would be converted to streptavidin-coated fibrils.
  • FBS fibril-biotin-streptavidin
  • a biotinylated anti-analyte antibody could be captured on the FBS support (either before or after the antibody has complexed to an analyte).
  • Assays using biotinylated anti-analyte antibodies are well established. Such assays include competitive assays where the analyte of interest competes with a labeled analyte for binding to the anti-analyte antibody.
  • Free (unbound) analyte and free (unbound) labeled analyte can be washed from the fibril immobilized antibody.
  • the washing step depends on the fibrils being physically separated from the solution phase by common practices involving centrifugation, filtration, or by attraction to a magnet.
  • a sandwich type immunoassay could be carried out on FBS supports. Sandwich immunoassays are well known in the field of diagnostics.
  • Such assays involve an analyte being bound simultaneously by two antibodies; a first "primary” antibody which is captured on a solid surface by for example being labeled with biotin, and a "secondary” antibody which is not captured by a solid surface but is labeled with a reporter group.
  • a sandwich assay could be carried out using fibrils as a solid capture support whereby the fibrils are captured as described in the previous paragraph.
  • the fibril would have covalently linked to it biotin, which would be bound to streptavidin, which would in turn be bound to a biotinylated primary antibody, which would be bound to analyte (if present), which would be bound to a labeled secondary antibody.
  • DNA probe assays could be carried out using FBS supports.
  • Biotinylated single stranded DNA can be bound to FBS supports and competitive hybridization can occur between complementary single stranded analyte DNA molecules and complementary labeled oligonucleotides.
  • biotinylated fibrils can be used in immunoassays and DNA probe assays.
  • bifunctional fibrils can be modified by covalent attachment of biotin to one type of functional group and alkyl chains to the other type of functional group.
  • the resultant alkylated, biotinylated fibrils can be used both in specific association with streptavidin or avidin (via biotin) and also for adsorption of proteins (via the alkyl chains).
  • Alkyl fibrils could be used in conjunction with other solid supports, such as streptavidin-coated magnetic beads.
  • One advantage of fibrils over such beads is that they have a much higher surface area (per unit weight). Thus, if fibrils could be attached to the outside surface of the magnetic beads, this would dramatically improve the surface area and hence the binding capacity of the beads.
  • alkylated, biotinylated fibrils Attorney DoTKet No. 100647-03591 63 could be mixed with streptavidin-coated beads resulting in high affinity streptavidin(bead)- biotin(fibril) interactions and hence fibril-coated beads with an extremely high surface area.
  • fibril-coated beads could be further derivatized with adsorbed proteins including streptavidin and antibodies.
  • streptavidin or antibody coated fibrils can be used in immunoassays and DNA probe assays.
  • fibril-coated beads could improve the properties of the beads by dramatically increasing their surface area such that fewer beads would be required in a given assay to give the same result.
  • the oxidized fibrils are more easily dispersed in aqueous media than unoxidized fibrils.
  • Stable, porous 3-dimensional structures with meso- and macropores (pores >2 nm) are very useful as catalysts or chromatography supports. Since fibrils can be dispersed on an individualized basis, a well-dispersed sample which is stabilized by crosslinks allows one to construct such a support.
  • Functionalized fibrils are ideal for this application since they are easily dispersed in aqueous or polar media and the functionality provides cross-link points. Additionally, the functionality provides points to support the catalytic or chromatographic sites. The end result is a rigid, 3-dimensional structure with its total surface area accessible with functional sites on which to support the active agent.
  • Typical applications for these supports in catalysis include their use as a highly porous support for metal catalysts laid down by impregnation, e.g., precious metal hydrogenation catalysts.
  • the ability to anchor molecular catalysts by tether to the support via the functionality combined with the very high porosity of the structure allows one to carry out homogeneous reactions in a heterogeneous manner.
  • the tethered molecular catalyst is essentially dangling in a continuous liquid phase, similar to a homogeneous reactor, in which it can make use of the advantages in selectivities and rates that go along with homogeneous reactions.
  • being tethered to the solid support allows easy separation and recovery of the active, and in many cases, very expensive catalyst.
  • the ligand on Co(II) containing the target molecule can then be recovered by mass action substitution of the labile Co(II) ligand, thereby effecting a separation and recovery of molecules which are otherwise very difficult or expensive to perform (e.g., chiral drugs).
  • the pores within the functionalized carbon fibril mats were too small to allow significant flow and thus would not be useful as flow through electrodes.
  • particulate carbon or other carbon based materials such as Reticulated Vitreous Carbon (RVC)
  • RVC Reticulated Vitreous Carbon
  • the porous electrode materials could not be formed in situ, packed too densely and formed voids or channels, were subject to dimensional instability during changes in solvent and flow conditions, and were unable to form very thin electrodes.
  • the use of functionalized carbon fibrils as electrodes in a flow cell solved such problems.
  • the functionalized carbon fibrils used as electrodes in a flow cell can be modified by surface treatment with electroactive agents.
  • the fibrils can also be modified with non-electroactive materials that may serve a catalytic or electrocatalytic function or serve to inhibit unwanted reactions or adsorption of materials from the flowing stream.
  • These flow through electrodes are useful in separation techniques such as electrochromatography, electrochemically modulated affinity chromatography, electrosynthesis or electrochemically modulated ion exchange chromatography. They can also be used in diagnostic devices that separate and/or analyze material trapped on the carbon fibril mat.
  • Composite mats composed of functionalized carbon fibrils and other fibers or particulates can also be used. These fibers or particulates can be added to the suspension to alter the final porosity or conductivity of the carbon fibril mat.
  • a electrochemical flow cell was constructed from a 13 mm, plastic, Swinney type membrane filter holder by placing a 13 mm diameter disk of gold mesh (400 mesh, Ladd Industries) on top of the membrane support and making electrical contact to the screen with a platinum wire, insulated with Teflon® heat shrink tubing that was fed through the wall of the filter holder for external connection as the working electrode of a three electrode potentiostat circuit.
  • the gold mesh was fixed in place with a minimal amount of epoxy around the outer edge.
  • a strip of gold foil was fashioned into a ring and placed in the bottom, down stream section of the filter holder and connected with an insulated Pt wire lead for connection as the counter electrode of a three electrode potentiostat circuit.
  • the flow cell was connected to a Sage syringe pump filled with 0.1M KCl in 0.1M potassium phosphate buffer at pH 7.0. Cyclic voltammograms (CVs) were recorded under no flow (static) and flow (0.4 mls/min.) at a potential scan rate of 20 mv/sec. (see Fig. 6).
  • nitric acid oxidized fibrils (185-01-02) was highly dispersed in 100 cc DI water using and U/S disintegrator.
  • the fibril slurry was heated to 90 0 C and a solution of 0.04 mol aluminum tributoxide dissolved in 20 cc propanol was slowly added. Reflux was continued for 4 hr, after which the condenser was removed to drive out the alcohol. After 30 min the condenser was put back and the slurry refluxed at 100 0 C overnight.
  • a black sol with uniform appearance was obtained.
  • the sol was cooled to RT and after one week, a black gel with a smooth surface was fo ⁇ ned.
  • the gel was heated at 300 0 C in air for 12 hr.
  • the alumina-fibril composites were examined by SEM. Micrographs of cracked surfaces showed a homogeneous dispersion of fibrils in the gel.
  • silica-fibril composites were examined by SEM. Micrographs of cracked surfaces showed a homogeneous dispersion of fibrils in the gel.
  • Polymer beads especially magnetic polymer beads containing an F ⁇ 3 ⁇ 4 core, such as those manufactured by Dynal and others, have many uses in diagnostics. These beads suffer, however, from having a low surface area compared to that available from nanotubes. Functionalized fibrils can be incorporated onto the surface of beads, which allows the polymer/fibril composites to be used as solid supports for separations or analytical application (e.g., electrochemiluminescence.assays, enzyme immobilization).
  • analytical application e.g., electrochemiluminescence.assays, enzyme immobilization
  • SWNT (University of Kentucky) were treated with 6M HCl for 72 hours to remove any metallic impurities. The acid washed nanotubes dispersed in DI water with sonication and filtered. This was repeated 4 times to rinse to a neutral pH.
  • the SWNT were resuspended in DI water and dispersed with sonication. 2X serial dilutions were made into 8 PP centrifuge tubes. Aliquots of methylene blue solution were added and the tubes placed on a rotator to agitate for 4 hours. The tubes were then spun in a centrifuge for 4 minutes resulting in the SWNT being pelleted at the bottom of the tubes. The tubes with the highest concentrations of SWNT had a clear filtrate and the two with the lowest SWNT concentration were similar in color to the control MB solution. The 6 tubes at intermediate SWNT concentrations showed increasing blue color as the concentration decreased.
  • SWNT (University of Kentucky) were treated with 6M HCl for 72 hours to remove any metallic impurities. The acid washed nanotubes dispersed in DI water with sonication and filtered. This was repeated 4 times to rinse to a neutral pH.
  • 7 mg of Fe Phthalocyanine - bis pyridine (FePc-2Py) was dissolved with 40 mis EtOH with sonication. 22 mg of SWNT were added and sonication continued for 5 minutes. Solution was allowed to cool and repeated sonication. Hot solution was filtered onto 0.45 micron PVDF membrane to dryness and then rinsed with fresh EtOH. Filtered to dryness. Dry weight 27 mg.
  • Electrodes were fashioned by pressing sections of the mat between 400 x 400 mesh SS mesh to serve as current collector. One edge of the SS mesh was attached to a Cu wire inserted into a glass pipette. Any exposed Cu was insulated with epoxy. The electrode was heated at IOOC for 1 hour to cure the 5 minute epoxy.
  • the electrode was examined by cyclic voltammetry vs a SS mesh counter and an Ag/AgCl reference electrode.
  • the electrolyte was isotonic borate buffered saline. Two peaks were observed, one near -.-4 that was obscured by the H2 evolution current. The second peak was centered about +0.1 V vs Ag/Ag/Cl. Peak currents for the peak centered at
  • FePc-2PY was strongly confined to the electrode and not lost to the electrolyte.
  • the invention has application in the formulation of a wide variety of functionalized nanotubes and uses therefor.

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Abstract

La présente invention se rapporte à des nanotubes de graphite, qui contiennent des fullerènes tubulaires (communément appelés 'buckytubes' en anglais) et des fibrilles, et qui sont fonctionnalisés par substitution chimique ou par adsorption de fractions fonctionnelles. Plus précisément, l'invention a trait à des nanotubes de carbone à simple paroi présentant un diamètre inférieur à 5 nanomètres, qui sont uniformément ou non uniformément substitués par des fractions chimiques ou sur lesquels sont adsorbés certains composés cycliques, ainsi qu'à des structures complexes constituées de tels nanotubes fonctionnalisés liés les uns aux autres. L'invention concerne aussi des procédés permettant d'introduire des groupes fonctionnels sur la surface de tels nanotubes. L'invention a également pour objet des procédés d'utilisation desdits nanotubes de carbone à simple paroi fonctionnalisés.
PCT/US2005/022413 2004-06-23 2005-06-23 Nanotubes de carbone a simple paroi fonctionnalises WO2006130150A2 (fr)

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CA002571575A CA2571575A1 (fr) 2004-06-23 2005-06-23 Nanotubes de carbone a simple paroi fonctionnalises
AU2005332329A AU2005332329A1 (en) 2004-06-23 2005-06-23 Functionalized single walled carbon nanotubes
EP05857879A EP1776125A4 (fr) 2004-06-23 2005-06-23 Nanotubes de carbone a simple paroi fonctionnalises
JP2007519302A JP2008513318A (ja) 2004-06-23 2005-06-23 官能基化単層カーボンナノチューブ

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US7947247B2 (en) 2005-03-29 2011-05-24 Hyperion Catalysis International, Inc. Method for preparing single walled carbon nanotubes from a metal layer
US8529862B2 (en) 2005-03-29 2013-09-10 Hyperion Catalysis International, Inc. Method for preparing single walled carbon nanotubes from a metal layer
US7951351B2 (en) 2006-03-29 2011-05-31 Hyperion Catalysis International, Inc. Method for preparing uniform single walled carbon nanotubes
WO2008156021A1 (fr) * 2007-06-21 2008-12-24 National University Corporation Nagoya University Procédé d'introduction d'une substance étrangère dans une cellule ayant une paroi cellulaire
US8420891B2 (en) 2007-06-21 2013-04-16 National University Corporation Nagoya University Method for introducing foreign substance into cell having cell wall
JPWO2008156021A1 (ja) * 2007-06-21 2010-08-26 国立大学法人名古屋大学 細胞壁を備える細胞に外来物質を導入する方法
JP4469959B2 (ja) * 2007-06-21 2010-06-02 国立大学法人名古屋大学 細胞壁を備える細胞に外来物質を導入する方法
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US8435931B2 (en) 2009-07-17 2013-05-07 Exxonmobil Research And Engineering Company Reduced friction lubricating oils containing functionalized carbon nanomaterials
US8841454B2 (en) 2009-07-17 2014-09-23 Exxonmobil Research And Engineering Company Functionalized carbon nanostructures which are soluble in hydrocarbons and method for preparation
JP2012096990A (ja) * 2011-11-02 2012-05-24 National Institute For Materials Science レドックスたんぱく質を非共有結合で結合させ機能化した生体反応性カーボンナノチューブの製法
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AU2005332329A1 (en) 2006-12-07
CA2571575A1 (fr) 2006-12-07
KR20070030282A (ko) 2007-03-15
CN101432227A (zh) 2009-05-13
WO2006130150A9 (fr) 2009-06-11
EP1776125A2 (fr) 2007-04-25
EP1776125A4 (fr) 2012-01-25
WO2006130150A3 (fr) 2009-04-16

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