Nanomedicine: Nanotechnology, Biology and Medicine
Volume 3, Issue 1 , Pages 53-62 , March 2007

Developing scanning probe–based nanodevices—stepping out of the laboratory into the clinic

Received 25 April 2006 ,Accepted 19 July 2006.

References 

  1. Feynman RP. There's Plenty of Room at the Bottom. In: A transcript of the classic talk that Richard Feynman gave on 29 December 1959 at the annual meeting of the American Physical Society. 1959;Available from: http://www.zyvex.com/nanotech/feynman.html/
  2. Binnig G, Rohrer H. Scanning tunnelling microscopy. Helv Phys Acta. 1982;55(6):726–735
  3. Binnig G, Quate CF, Gerber C. Atomic force microscope. Phys Rev Lett. 1986;56(9):930–933
  4. Medalia O, Weber I, Frangakis AS, Nicastro D, Gerisch G, Baumeister W, et al. Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography. Science. 2002;298:1209–1213
  5. Steven AC, Aebi U. The next ice age: cryo-electron tomography of intact cells. Trends Cell Biol. 2003;13:107–110
  6. Lucic V, Forster F, Baumeister W. Structural studies by electron tomography: from cells to molecules. Annu Rev Biochem. 2005;74:833–865
  7. Hoenger A, Aebi U. 3-D reconstructions from ice-embedded and negatively stained biomacromolecular assemblies: a critical comparison. J Struct Biol. 1996;117:99–116
  8. Czajkowsky DM, Hotze EM, Shao Z, Tweten RK. Vertical collapse of a cytolysin prepore moves its transmembrane (-hairpins to the membrane. EMBO J. 2004;23:3206–3215
  9. Karrasch S, Hegerl R, Hoh JH, Baumeister W, Engel A. Atomic force microscopy produces faithful high-resolution images of protein surfaces in an aqueous environment. Proc Natl Acad Sci U S A. 1994;91:836–838
  10. Mou J, Yang J, Shao Z. Atomic force microscopy of cholera toxin B-oligomers bound to bilayers of biologically relevant lipids. J Mol Biol. 1995;248:507–512
  11. Muller DJ, Sass HJ, Muller SA, Buldt G, Engel A. Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane. J Mol Biol. 1999;285:1903–1909
  12. Muller DJ, Schoenenberger CA, Schabert F, Engel A. Structural changes in native membrane proteins monitored at subnanometer resolution with the atomic force microscope: a review. J Struct Biol. 1997;119:149–157
  13. Reviakine II, Bergsma-Schutter W, Brisson A. Growth of protein 2-D crystals on supported planar lipid bilayers imaged in situ by AFM. J Struct Biol. 1998;121:356–361
  14. Sanner M, Stolz M, Burkhard P, Kong XP, Min G, Sun TT, et al. Visualizing nature at work from the nano to the macro scale. Nanobiotechnol. 2005;1:7–22
  15. Schabert FA, Henn C, Engel A. Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy. Science. 1995;268:92–94
  16. Scheuring S, Ringler P, Borgnia M, Stahlberg H, Muller DJ, Agre P, et al. High-resolution AFM topographs of the Escherichia coli water channel aquaporin Z. EMBO J. 1999;18:4981–4987
  17. Fotiadis D, Liang Y, Filipek S, Saperstein DA, Engel A, Palczewski K, et al. Atomic-force microscopy: rhodopsin dimers in native disc membranes. Nature. 2003;421:127–128
  18. Stolz M, Stoffler D, Aebi U, Goldsbury C. Monitoring biomolecular interactions by time-lapse atomic force microscopy. J Struct Biol. 2000;131:171–180
  19. Viani MB, Schaffer TE, Paloczi GT, Pietrasanta I, Smith BL, Thompson JB, et al. Fast imaging and fast force spectroscopy of single biopolymers with a new atomic force microscope designed for small cantilevers. Rev Sci Instrum. 1999;70(11):4300–4303
  20. Ando T, Kodera N, Naito Y, Kinoshita T, Furuta K, Toyoshima YY, et al. A high-speed atomic force microscope for studying biological macromolecules in action. Chem Phys Chem. 2003;4:1196–1202
  21. Kodera N, Kinoshita T, Ito T, Ando T. High-resolution imaging of myosin motor in action by a high-speed atomic force microscope. Adv Exp Med Biol. 2003;538:119–127
  22. Kindt JH, Fantner GE, Cutroni JA, Hansma PK. Rigid design of fast scanning probe microscopes using finite element analysis. Ultramicroscopy. 2004;100:259–265
  23. Schitter G, Stark RW, Stemmer A. Fast contact-mode atomic force microscopy on biological specimen by model-based control. Ultramicroscopy. 2004;100:253–257
  24. Hoenger A, Sablin EP, Vale RD, Fletterick RJ, Milligan RA. Three-dimensional structure of a tubulin-motor-protein complex. Nature. 1995;376:271–274
  25. Hirokawa N, Takemura R. Molecular motors and mechanisms of directional transport in neurons. Nat Rev Neurosci. 2005;6:201–214
  26. Yildiz A, Selvin PR. Kinesin: walking, crawling or sliding along?. Trends Cell Biol. 2005;15:112–120
  27. Wang H, Oster G. Energy transduction in the F1 motor of ATP synthase. Nature. 1998;396:279–282
  28. Rondelez Y, Tresset G, Nakashima T, Kato-Yamada Y, Fujita H, Takeuchi S, et al. Highly coupled ATP synthesis by F1-ATPase single molecules. Nature. 2005;433:773–777
  29. Stoffler D, Goldie KN, Feja B, Aebi U. Calcium-mediated structural changes of native nuclear pore complexes monitored by time-lapse atomic force microscopy. J Mol Biol. 1999;287:741–752
  30. Yellen G. The voltage-gated potassium channels and their relatives. Nature. 2002;419:35–42
  31. Jones SW. Calcium channels: unanswered questions. J Bioenerg Biomembr. 2003;35:461–475
  32. Doyle DA. Structural themes in ion channels. Eur Biophys J. 2004;33:175–179
  33. Walz T, Haner M, Wu XR, Henn C, Engel A, Sun TT, et al. Towards the molecular architecture of the asymmetric unit membrane of the mammalian urinary bladder epithelium: a closed “twisted ribbon” structure. J Mol Biol. 1995;248:887–900
  34. Kachar B, et al. Three-dimensional analysis of the 16 nm urothelial plaque particle: luminal surface exposure, preferential head-to-head interaction, and hinge formation. J Mol Biol. 1999;285:595–608
  35. Oostergetel GT, Keegstra W, Brisson A. Structure of the major membrane protein complex from urinary bladder epithelial cells by cryo-electron crystallography. J Mol Biol. 2001;314:245–252
  36. Min G, Stolz M, Zhou G, Liang F, Sebbel P, Stoffler D, et al. Localization of uroplakin Ia, the urothelial receptor for bacterial adhesion FimH, on the six inner domains of the 16 nm urothelial plaque particle. J Mol Biol. 2002;317:697–706
  37. Sun TT, Liang FX, Wu XR. Uroplakins as markers of urothelial differentiation. Adv Exp Med Biol. 1999;462:7–18
  38. Hooton TM, Stamm WE. Diagnosis and treatment of uncomplicated urinary tract infection. Infect Dis Clin North Am. 1997;11:551–581
  39. Steinmetz MO, Goldie KN, Aebi U. A correlative analysis of actin filament assembly, structure, and dynamics. J Cell Biol. 1997;138:559–574
  40. Steinmetz MO, Stoffler D, Hoenger A, Bremer A, Aebi U. Actin: from cell biology to atomic detail. J Struct Biol. 1997;119:295–320
  41. Schoenenberger CA, Steinmetz MO, Stoffler D, Mandinova A, Aebi U. Structure, assembly, and dynamics of actin filaments in situ and in vitro. Microsc Res Tech. 1999;47:38–50
  42. Ando T, Kodera N, Takai E, Maruyama D, Saito K, Toda A, et al. A high-speed atomic force microscope for studying biological macromolecules. Proc Natl Acad Sci U S A. 2001;98:12468–12472
  43. Fahrenkrog B, Aebi U. The nuclear pore complex: nucleocytoplasmic transport and beyond. Nat Rev Mol Cell Biol. 2003;4:757–766
  44. Stoffler D, et al. Cryo-electron tomography provides novel insights into nuclear pore architecture: implications for nucleocytoplasmic transport. J Mol Biol. 2003;328:119–130
  45. Jarnik M, Aebi U. Toward a more complete 3-D structure of the nuclear pore complex. J Struct Biol. 1991;107:291–308
  46. Aebi U, Cohn J, Buhle L, Gerace L. The nuclear lamina is a meshwork of intermediate-type filaments. Nature. 1986;323:560–564
  47. Panté N, Aebi U. Toward the molecular dissection of protein import into nuclei. Curr Opin Cell Biol. 1996;8:397–406
  48. Stolz M, et al. Dynamic elastic modulus of porcine articular cartilage determined at two different levels of tissue organization by indentation-type atomic force microscopy. Biophys J. 2004;86:3269–3283
  49. Ross R. The pathogenesis of atherosclerosis—an update. N Engl J Med. 1986;314:488–500
  50. Naghavi M, Libby P, Falk E, Casscells SW, Litovsky S, Rumberger J, et al. From vulnerable plaque to vulnerable patient: a call for new definitions and risk assessment strategies: Part II. Circulation. 2003;108:1772–1778
  51. Naghavi M, Libby P, Falk E, Casscells SW, Litovsky S, Rumberger J, et al. From vulnerable plaque to vulnerable patient: a call for new definitions and risk assessment strategies: Part I. Circulation. 2003;108:1664–1672
  52. Libby P. Vascular biology of atherosclerosis: overview and state of the art. Am J Cardiol. 2003;91:3A–6A
  53. Libby P, Theroux P. Pathophysiology of coronary artery disease. Circulation. 2005;111:3481–3488
  54. Virmani R, Kolodgie FD, Burke AP, Farb A, Schwartz SM. Lessons from sudden coronary death: a comprehensive morphological classification scheme for atherosclerotic lesions. Arterioscler Thromb Vasc Biol. 2000;20:1262–1275
  55. Reichlin T, Wild A, Durrenberger M, Daniels AU, Aebi U, Hunziker PR, et al. Investigating native coronary artery endothelium in situ and in cell culture by scanning force microscopy. J Struct Biol. 2005;152:52–63
  56. Tkaczuk H. Human cartilage stiffness. In vivo studies. Clin Orthop. 1986;206:301–312
  57. Lyyra T, Jurvelin J, Pitkanen P, Vaatainen U, Kiviranta I. Indentation instrument for the measurement of cartilage stiffness under arthroscopic control. Med Eng Phys. 1995;17:395–399
  58. Shepherd DE, Seedhom BB. A technique for measuring the compressive modulus of articular cartilage under physiological loading rates with preliminary results. Proc Inst Mech Eng [H]. 1997;211:155–165
  59. Appleyard RC, Swain MV, Khanna S, Murrell GA. The accuracy and reliability of a novel handheld dynamic indentation probe for analysing articular cartilage. Phys Med Biol. 2001;46:541–550
  60. Stolz M, Imer R, Staufer U, Aebi U. Nanotechnology on the verge of stepping into the clinic: development of an arthroscopic AFM. BioWorld. 2003;4:2–5
  61. Leinhos T, Rudow O, Stopka M, Vollkopf A, Oesterschulze E. Coaxial probes for scanning near-field microscopy. J Microsc. 1999;194:349–352
  62. Eckert R, Freyland JM, Gersen H, Heinzelmann H, Schurmann G, Noell W, et al. Near-field optical microscopy based on microfabricated probes. J Microsc. 2001;202:7–11
  63. Khodjakov A, Cole RW, Rieder CL. A synergy of technologies: combining laser microsurgery with green fluorescent protein tagging. Cell Motil Cytoskeleton. 1997;38:311–317
  64. Sacconi L, Tolic-Norrelykke IM, Antolini R, Pavone FS. Combined intracellular three-dimensional imaging and selective nanosurgery by a nonlinear microscope. J Biomed Opt. 2005;10:14002
  65. Colombelli J, Reynaud EG, Rietdorf J, Pepperkok R, Stelzer EH. In vivo selective cytoskeleton dynamics quantification in interphase cells induced by pulsed ultraviolet laser nanosurgery. Traffic. 2005;6:1093–1102
  66. Miles M. Scanning probe microscopy. Probing the future. Science. 1997;277:1845–1847
  67. Menger FM. Supramolecular chemistry and self-assembly. Proc Natl Acad Sci U S A. 2002;99:4818–4822
  68. Eckel R, Ros R, Decker B, Mattay J, Anselmetti D. Supramolecular chemistry at the single-molecule level. Angew Chem Int Ed Engl. 2005;44:484–488
  69. Frederix PL, Gullo MR, Akiyama T, Tonin A, Rooij NF, Staufer U, et al. Assessment of insulated conductive cantilevers for biology and electrochemistry. Nanotechnology. 2005;16:997–1005
  70. Cannaerts M, Chamirian O, Maex K, Van Haesendonck C. Mapping nanometre-scale temperature gradients in patterned cobalt-nickel silicide films. Nanotechnology. 2002;13:149–152
  71. Aszodi A, Pfeifer A, Wendel M, Hiripi L, Fassler R. Mouse models for extracellular matrix diseases. J Mol Med. 1998;76:238–252
  72. Helminen HJ, Saamanen AM, Salminen H, Hyttinen MM. Transgenic mouse models for studying the role of cartilage macromolecules in osteoarthritis. Rheumatology (Oxford). 2002;41:848–856
  73. Fournier C. Where do T cells stand in rheumatoid arthritis?. Joint Bone Spine. 2005;72:527–532
  74. Korhonen RK, Laasanen MS, Toyras J, Lappalainen R, Helminen HJ, Jurvelin JS, et al. Fibril reinforced poroelastic model predicts specifically mechanical behavior of normal, proteoglycan depleted and collagen degraded articular cartilage. J Biomech. 2003;36:1373–1379
  75. Basalo IM, Mauck RL, Kelly TA, Nicoll SB, Chen FH, Hung CT, et al. Cartilage interstitial fluid load support in unconfined compression following enzymatic digestion. J Biomech Eng. 2004;126:779–786
  76. Saad OM, Myers RA, Castleton DL, Leary JA. Analysis of hyaluronan content in chondroitin sulfate preparations by using selective enzymatic digestion and electrospray ionization mass spectrometry. Anal Biochem. 2005;344:232–239
  77. Hunziker P, Stolz M, Aebi U. Nanotechnology in medicine: moving from the bench to the bedside. Chimia. 2002;56:520–526
  78. Langer R, Vacanti JP. Tissue engineering. Science. 1993;260:920–926

 No conflict of interest was reported by the authors of this paper.

PII: S1549-9634(07)00002-0

doi: 10.1016/j.nano.2007.01.001

Nanomedicine: Nanotechnology, Biology and Medicine
Volume 3, Issue 1 , Pages 53-62 , March 2007