Biological control of nanoparticles

• US 20030113714A1
• Filed: 09/25/2002
• Published: 06/19/2003
• Est. Priority Date: 09/28/2001
• Status: Abandoned Application

• Current Assignee: Rice University, Board of Regents of the University of Texas System (University of Texas System)
• Original Assignee: Board of Regents of the University of Texas System (University of Texas System)
• Inventors: Smalley, Richard E., Belcher, Angela M., Lee, Seung-Wuk, Ryan, Esther
• Application Number:
  US10/254,446
• Publication Number:
  US 20030113714A1
• Time in Patent Office: Days
• US Class Current: 435/5
• CPC Class Codes: A61P 35/00 Antineoplastic agents
• CPC Class Codes: A61P 9/00 Drugs for disorders of the cardiovascular system
• CPC Class Codes: B01J 2219/005 Beads
• CPC Class Codes: B82Y 10/00 Nanotechnology for information processing, storage or transmission, e.g. quantum computing or single electron logic
• CPC Class Codes: C07B 2200/11 Compounds covalently bound to a solid support
• CPC Class Codes: C07K 1/047 Simultaneous synthesis of different peptide species; Peptide libraries
• CPC Class Codes: C07K 7/06 having 5 to 11 amino acids
• CPC Class Codes: C07K 7/08 having 12 to 20 amino acids gastrins C07K14/595; somatostatins C07K14/655; melanotropins C07K14/68
• CPC Class Codes: C12N 15/1037 Screening libraries presented on the surface of microorganisms, e.g. phage display, E. coli display
• CPC Class Codes: C40B 40/02 Libraries contained in or displayed by microorganisms, e.g. bacteria or animal cells; Libraries contained in or displayed by vectors, e.g. plasmids; Libraries containing only microorganisms or vectors
• CPC Class Codes: G01N 33/54373 involving physiochemical end-point determination, e.g. wave-guides, FETS, gratings
• CPC Class Codes: G01N 33/54386 Analytical elements
• CPC Class Codes: G01N 33/551 the carrier being inorganic
• CPC Class Codes: H10K 10/701 Organic molecular electronic devices
• CPC Class Codes: H10K 85/761 Biomolecules or bio-macromolecules, e.g. proteins, chlorophyl, lipids or enzymes

Abstract

The present invention includes compositions and methods for selective binding of amino acid oligomers to semiconductor and elemental carbon-containing materials. One form of the present invention is a method for controlling the particle size of the semiconductor or elemental carbon-containing material by interacting an amino acid oligomer that specifically binds the material with solutions that can result in the formation of the material. The same method can be used to control the aspect ratio of the nanocrystal particles of the semiconductor material. Another form of the present invention is a method to create nanowires from the semiconductor or elemental carbon-containing material. Yet another form of the present invention is a biologic scaffold comprising a substrate capable of binding one or more biologic materials, one or more biologic materials attached to the substrate, and one or more elemental carbon-containing molecules attached to one or more biologic materials.

Claims

1. A method for directed semiconductor formation comprising the steps of:

contacting a polymeric organic material that binds a predetermined face specificity semiconductor material with a first ion to create a semiconductor material precursor; and

adding a second ion to the semiconductor material precursor, wherein the polymeric organic material directs formation of the predetermined face specificity semiconductor material.

2. The method of claim 1, wherein the polymeric organic material is an amino acid oligomer.

3. The method of claim 1, wherein the polymeric organic material is an amino acid oligomer on the surface of a bacteriophage.

4. The method of claim 1, wherein the polymeric organic material is an amino acid oligomer displayed on the surface of bacteria.

5. The method of claim 1, wherein the polymeric organic material is an amino acid oligomer displayed on the surface of cell as a label.

6. The method of claim 1, wherein the polymeric organic material is a nucleic acid oligomer.

7. The method of claim 1, wherein the polymeric organic material is a combinatorial library.

8. The method of claim 1, wherein the polymeric organic material comprises amino acid polymers of between about 7 and 20 amino acids.

9. The method of claim 1, wherein the predetermined face specificity semiconductor material is polycrystalline.

10. The method of claim 1, wherein the predetermined face specificity semiconductor material is single crystalline.

11. The method of claim 1, wherein the predetermined face specificity semiconductor material comprises a Group II-IV semiconductor material.

12. The method of claim 1, wherein the polymeric organic material comprises a chimeric protein.

13. The method of claim 1, wherein the polymeric organic material comprises a chimeric protein and wherein the portion of the chimeric protein that binds the semiconductor material is on the surface of the chimeric protein.

14. The method of claim 1, wherein the polymeric organic material comprises a chimeric protein and wherein the portion of the chimeric protein that binds the semiconductor material comprises between about 7 and 20 amino acids.

15. The method of claim 1, wherein the polymeric organic material nucleates size constrained crystalline semiconductor materials.

16. The method of claim 1, wherein the polymeric organic material controls the crystallographic phase of nucleated nanoparticles of the semiconductor.

17. The method of claim 1, wherein the polymeric organic material controls the aspect ratio of the nanocrystals of the semiconductor.

18. The method of claim 1, wherein the polymeric organic material controls the dopant levels of the semiconductor nanocrystals formed.

49. A semiconductor made using the process of claim 1.

50. A semiconductor material made using the process of claim 15.

19. A method for directed semiconductor formation comprising the steps of:

contacting a peptide that binds a predetermined face specificity semiconductor material with a first ion to create a semiconductor material precursor; and

adding a second ion to the semiconductor material precursor, wherein the peptide directs formation of the predetermined face specificity semiconductor material.

20. The method of claim 19, wherein the peptide is on the surface of a bacteriophage.

21. The method of claim 19, wherein the peptide is part of a combinatorial library.

22. The method of claim 19, wherein the peptide comprises between about 7 and 20 amino acids.

23. The method of claim 19, wherein the predetermined face specificity semiconductor material is polycrystalline.

24. The method of claim 19, wherein the predetermined face specificity semiconductor material is single crystalline.

25. The method of claim 19, wherein the predetermined face specificity semiconductor material comprises a Group II-VI semiconductor material.

26. The method of claim 19, wherein the polymeric organic material is displayed on the surface of bacteria.

27. The method of claim 19, wherein the polymeric organic material is displayed on the surface of cell as a label.

28. The method of claim 19, wherein the peptide comprises a chimeric protein.

29. The method of claim 19, wherein the peptide comprises a chimeric protein and wherein the peptide portion of the chimeric protein that binds the semiconductor material is on the surface of the chimeric protein.

30. The method of claim 19, wherein the peptide comprises a chimeric protein and wherein the portion of the chimeric protein that binds the semiconductor material comprises between about 7 and 20 amino acids.

31. The method of claim 19, wherein the peptide nucleates size constrained crystalline semiconductor materials.

32. The method of claim 19, wherein the peptide controls the crystallographic phase of nucleated nanoparticles of the semiconductor.

33. The method of claim 19, wherein the peptide is selected from a 12 mer linear library.

34. The method of claim 19, wherein the peptide is selected from a 7 mer constrained library.

35. A method for nucleating semiconductor material comprising the steps of:

selecting a peptide that binds to a predetermined face specificity material;

preparing a portion of a gold surface that has been altered to have the peptide attached to the surface;

contacting the gold surface-peptide complex with a first ion needed for semiconductor crystal precursor formation; and

adding a second ions needed for semiconductor crystal formation.

36. The method of claim 35, wherein the peptide is selected from a constrained library.

37. The method of claim 35, wherein the gold-surface is prepared by forming a self-assembled monolayer with 2-mercaptoethylamine on the gold substrate.

38. The method of claim 35, wherein the predetermined face specificity semiconductor material comprises a Group II-VI semiconductor material.

39. The method of claim 35, wherein the semiconductor material is zinc sulfide and the solutions are zinc chloride and sodium sulfide.

40. The method of claim 35, wherein the semiconductor material is cadmium sulfide and the solutions are cadmium chloride and sodium sulfide.

41. The method of claim 35, wherein the peptide is selected by combinatorial library screening.

51. A nanowire made using the process of claim 35.

42. A method of constructing nanowires comprising the steps of:

selecting peptides that bind a predetermined face specificity semiconductor material; and

expressing the peptides as a fusion protein with a protein that is capable of self-assembly;

then interact fused with semiconductor precusors to direct formation of semiconductor nanocrystals.

43. The method of claim 42, wherein the peptides selected are expressed in high copy number.

44. The method of claim 42, wherein the self-assembled protein is on the surface of a bacteriophage.

45. The method of claim 42, wherein the polymeric organic material is displayed on the surface of bacteria.

46. The method of claim 42, wherein the polymeric organic material is displayed on the surface of cell as a label.

47. The method of claim 42, wherein the self-assembled protein comprises a portion of the major coat protein of M1 bacteriophage.

48. The method of claim 42, wherein the self-assembled protein comprises a portion of the p8 major coat protein of M1 bacteriophage.

52. A biologic scaffold comprising:

a substrate capable of binding one or more biologic materials;

one or more biologic materials attached to the substrate; and

one or more elemental carbon-containing molecules attached to one or more biologic materials.

53. The biologic scaffold of claim 52, wherein the substrate is selected from the group consisting of silicon, Langmuir-Bodgett films, functionalized glass, germanium, ceramic, silicon, a semiconductor material, PTFE, carbon, polycarbonate, mica, mylar, plastic, quartz, polystyrene, gallium arsenide, gold, silver, metal, metal alloy, fabric, tissue, cell, organ, protein, antibody, and combinations thereof.

54. The biologic scaffold of claim 52, wherein the biologic material is selected from the group consisting of virus, bacteriophage, bacteria, peptide, protein, amino acid, steroid, drug, chromophore, antibody, enzyme, single-stranded or double-stranded nucleic acid, nucleic acid polymer, and any chemical modifications thereof.

55. The biologic scaffold of claim 52, wherein the biologic material is identified by a combinatorial library screening.

56. The biologic scaffold of claim 52, wherein the biologic material is an amino acid oligomer present on the surface of a bacteriophage.

57. The biologic scaffold of claim 52, wherein the biologic material is an amino acid oligomer displayed on the surface of bacteria.

58. The biologic scaffold of claim 52, wherein the biologic material is an amino acid oligomer between 7 and 20 amino acids long.

59. The biologic scaffold of claim 52, wherein the biologic material is a peptide on the surface of a bacteriophage.

60. The biologic scaffold of claim 59, wherein the biologic material is a peptide selected from the group consisting of SEQ ID NO.:

105-245.

61. The biologic scaffold of claim 52, wherein the elemental carbon-containing molecule recognizes a peptide selected from the group consisting of SEQ ID NO.:

105-245.

62. The biologic scaffold of claim 52, wherein the elemental carbon-containing molecule is selected from the group consisting of carbon₆₀, carbon planchet, highly ordered pyrolytic graphite, single-walled nanotube paste, single-walled nanotube, multi-walled nanotube, multi-walled nanotube paste, diamond, graphite, activated carbon, carbon black, industrial carbon, charcoal, coke, steel, carbon cycle, and combinations thereof.

63. The biologic scaffold of claim 52, wherein the substrate is absent from the biologic scaffold.

64. The biologic scaffold of claim 52, wherein the biologic scaffold is used for applications selected from the group consisting of synthesis of elemental carbon-containing materials, carbon nanutube alignment, creation of biologic semiconductors, junction conversion for single-walled nanotube paste, junction conversion for multi-walled nanotube paste, enhancing solubility and biologic compatability of single- and multi-walled nanotube paste, producing an integrated single- and multi-walled nanotube paste, biosensor production, release of pharmaceutical compositions, treatment of cancer, and combinations thereof.

107. An integrated circuit derived from the biologic scaffold of claim 52.

108. A biosensor derived from the biologic scaffold of claim 52.

109. A drug delivery system using the biologic scaffold of claim 52.

111. A treatment for cancer using the biologic scaffold of claim 52.

65. A biologic scaffold comprising:

a substrate capable of binding one or more biologic materials;

a biologic material attached to the substrate and an organic polymer attached to the biologic material; and

one or more elemental carbon-containing molecules attached to the organic polymer.

66. The biologic scaffold of claim 65, wherein the substrate is selected from the group consisting of silicon, Langmuir-Bodgett films, functionalized glass, germanium, ceramic, silicon, a semiconductor material, PTFE, carbon, polycarbonate, mica, mylar, plastic, quartz, polystyrene, gallium arsenide, gold, silver, metal, metal alloy, fabric, tissue, cell, organ, protein, antibody, and combinations thereof.

67. The biologic scaffold of claim 65, wherein the biologic material is selected from the group consisting of virus, bacteriophage, bacteria, peptide, protein, amino acid, steroid, drug, chromophore, antibody, enzyme, single-stranded or double-stranded nucleic acid, nucleic acid polymer, and any chemical modifications thereof.

68. The biologic scaffold of claim 65, wherein the biologic material and organic polymer are the same.

69. The biologic scaffold of claim 65, wherein the organic polymer is a protein, antibody, peptide, nucleic acid, chimeric molecule, drug, label, other carbon-containing organic materials known to exist in eukaryotic organisms, and derivatives or analogs of biologic polymers that contain one or more biologic monomers in combinations with synthetic monomers that mimic those found naturally.

70. The biologic scaffold of claim 65, wherein the organic polymer is identified by a combinatorial library screening.

71. The biologic scaffold of claim 65, wherein the organic polymer is an amino acid oligomer between 7 and 20 amino acids long.

72. The biologic scaffold of claim 65, wherein the organic polymer is a peptide that recognizes a select portion of the biologic material

73. The biologic scaffold of claim 65, wherein the second biologic material is a peptide selected from the group consisting of SEQ ID NO.:

105-245.

74. The biologic scaffold of claim 65, wherein the elemental carbon-containing molecule recognizes a peptide selected from the group consisting of SEQ ID NO.:

105-245.

75. The biologic scaffold of claim 65, wherein the elemental carbon-containing molecule is selected from the group consisting of carbon₆₀, carbon planchet, highly ordered pyrolytic graphite, single-walled nanotube paste, single-walled nanotube, multi-walled nanotube, multi-walled nanotube paste, diamond, graphite, activated carbon, carbon black, industrial carbon, charcoal, coke, steel, carbon cycle, and combinations thereof.

76. The biologic scaffold of claim 65, wherein the biologic scaffold is used for applications selected from the group consisting of synthesis of elemental carbon-containing materials, carbon nanutube alignment, creation of biologic semiconductors, junction conversion for single-walled nanotube paste, junction conversion for multi-walled nanotube paste, enhancing solubility and biologic compatability of single- and multi-walled nanotube paste, producing an integrated single- and multi-walled nanotube paste, biosensor production, release of pharmaceutical compositions, treatment of cancer, and combinations thereof.

77. The biologic scaffold of claim 65, wherein the substrate and the biologic material are the same.

78. A biologic scaffold comprising:

a substrate capable of binding one or more bacteriophages;

one or more bacteriophages attached to the substrate;

one or more peptides that recognize a portion of the bacteriophage; and

one or more elemental carbon-containing molecules that recognize the peptide.

79. The biologic scaffold of claim 78, wherein the substrate is silicon, Langmuir-Bodgett films, functionalized glass, germanium, ceramic, silicon, a semiconductor material, PTFE, carbon, polycarbonate, mica, mylar, plastic, quartz, polystyrene, gallium arsenide, gold, silver, metal, metal alloy, fabric, tissue, cell, organ, protein, antibody, and combinations thereof.

80. The biologic scaffold of claim 78, wherein the peptide is selected from the group consisting of SEQ ID NO.:

105-245.

81. The biologic scaffold of claim 78, wherein the elemental carbon-containing molecule is selected from the group consisting of carbon₆₀, carbon planchet, highly ordered pyrolytic graphite, single-walled nanotube paste, single-walled nanotube, multi-walled nanotube, multi-walled nanotube paste, diamond, graphite, activated carbon, carbon black, industrial carbon, charcoal, coke, steel, carbon cycle, and combinations thereof.

82. The biologic scaffold of claim 78, wherein the peptide is selected from the group consisting of drug, antibody, chromophore, light-emitting label, light absorbing label, and organic polymer.

83. The biologic scaffold of claim 78, wherein the substrate is absent.

84. A method of making a biologic scaffold comprising:

providing a substrate capable of binding one or more biologic materials;

attaching one or more biologic materials to the substrate; and

contacting one or more elemental carbon-containing molecules with the biologic material to form a biologic scaffold.

85. The method of claim 84, wherein the substrate is selected from the group consisting of silicon, Langmuir-Bodgett films, functionalized glass, germanium, ceramic, silicon, a semiconductor material, PTFE, carbon, polycarbonate, mica, mylar, plastic, quartz, polystyrene, gallium arsenide, gold, silver, metal, metal alloy, fabric, tissue, cell, organ, protein, antibody, and combinations thereof.

86. The method of claim 84, wherein the biologic material is selected from the group consisting of virus, bacteriophage, bacteria, peptide, protein, amino acid, steroid, drug, chromophore, label, antibody, enzyme, single-stranded or double-stranded nucleic acid, nucleic acid polymer, chimeric molecule, drug, any other carbon-containing materials known to exist in eukaryotic organisms, and derivatives or analogs of biologic polymers that contain one or more biologic monomers in combination with synthetic monomers that mimic those found naturally.

87. The method of claim 84, wherein the biologic material is identified by combinatorial library screening.

88. The method of claim 84, wherein the biologic material is an amino acid oligomer on the surface of a bacteriophage.

89. The method of claim 84, wherein the biologic material is a peptide displayed on the surface of bacteria.

90. The method of claim 88, wherein the amino acid oligomer is between 7 and 20 amino acids long.

91. The method of claim 89, wherein the peptide is selected from the group consisting of SEQ ID NO.:

105-245.

92. The method of claim 89, wherein the peptide is selected from the group consisting of drug, antibody, chromophore, light-emitting label, light absorbing label, and organic polymer.

93. The method of claim 84, wherein the elemental carbon-containing molecule recognizes a peptide selected from the group consisting of SEQ ID NO.:

105-245.

94. The method of claim 84, wherein the elemental carbon-containing molecule is selected from the group consisting of carbon₆₀, carbon planchet, highly ordered pyrolytic graphite, single-walled nanotube paste, single-walled nanotube, multi-walled nanotube, multi-walled nanotube paste, diamond, graphite, activated carbon, carbon black, industrial carbon, charcoal, coke, steel, carbon cycle, and combinations thereof.

95. The method of claim 84, wherein providing a substrate capable of binding one or more biologic materials and attaching one or more biologic materials to the substrate are not required to make the biologic scaffold.

96. A molecule comprising:

an organic polymer, wherein the organic polymer selectively recognizes an elemental carbon-containing molecule.

97. The molecule of claim 96, wherein the molecule is used for applications selected from the group consisting of synthesis of elemental carbon-containing materials, carbon nanutube alignment, creation of biologic semiconductors, junction conversion for single-walled nanotube paste, junction conversion for multi-walled nanotube paste, enhancing solubility and biologic compatability of single- and multi-walled nanotube paste, producing an integrated single- and multi-walled nanotube paste, biosensor production, release of pharmaceutical compositions, treatment of cancer, and combinations thereof.

98. The molecule of claim 96, wherein the organic polymer is a nucleic acid oligomer.

99. The molecule of claim 96, wherein the organic polymer is selected by a combinatorial library screening.

100. The molecule of claim 96, wherein the organic polymer is an amino acid oligomer on the surface of a bacteriophage.

101. The molecule of claim 100, wherein the amino acid oligomer is displayed on the surface of bacteria.

102. The molecule of claim 100, wherein the amino acid oligomer is between 7 and 15 amino acids long.

103. The molecule of claim 96, wherein the organic polymer is a peptide on the surface of a bacteriophage.

104. The molecule of claim 103, wherein the peptide is selected from the group consisting of SEQ ID NO.:

105-245.

105. The molecule of claim 96, wherein the elemental carbon-containing molecule recognizes a peptide selected from the group consisting of SEQ ID NO.:

105-245.

106. The molecule of claim 96, wherein the elemental carbon-containing molecule is selected from the group consisting of carbon₆₀, carbon planchet, highly ordered pyrolytic graphite, single-walled nanotube paste, single-walled nanotube, multi-walled nanotube, multi-walled nanotube paste, diamond, graphite, activated carbon, carbon black, industrial carbon, charcoal, coke, steel, carbon cycle, and combinations thereof.

110. A pharmaceutical composition using a pharmaceutically effective amount of the molecule of claim 96.

112. A method for separating metallic and semi-conducting nanotubes comprising the steps of:

obtaining protein sequences using a combinatorial library screening that distinguishes metallic and semi-conducting nanotubes;

contacting a mixture of metallic and semi-conducting nanotubes with the obtained protein sequences; and

p1 separating the semi-conducting nanotube from the metallic nanotube

113. The method of claim 112, wherein metallic and semi-conducting nanotubes are selected from the group consisting of single-walled nanotubes and multi-walled nanotubes.