Analytical tools for detecting amyloid beta oligomerisation and assembly

Current Pharmaceutical Analysis

Volumn 5, Issue 3, 2009, Pages 229-245

  Vestergaard, Mun'delanji ^a   Kerman, Kagan ^b  

^a JAPAN ADVANCED INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^b UNIVERSITY OF TORONTO   (Canada)

Author keywords

Amyloid beta; Assembly; Detection tools; Kinetics; Nanotechnology; Oligomerisation

Indexed keywords

AMYLOID BETA PROTEIN;

AGAR GEL ELECTROPHORESIS; ALZHEIMER DISEASE; BETA SHEET; CIRCULAR DICHROISM; ELECTROCHEMICAL ANALYSIS; FLUORESCENCE SPECTROSCOPY; HUMAN; LIGHT SCATTERING; NANOTECHNOLOGY; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN POLYMERIZATION; REVIEW; SENSITIVITY AND SPECIFICITY; SURFACE PLASMON RESONANCE;

EID: 70649110747     PISSN: 15734129     EISSN: None     Source Type: Journal    
DOI: 10.2174/157341209788922039     Document Type: Review

References (156)

1. World Health Organisation, Aug, 2006: http://www.searo.who.int/EN/ Section1174/Section1199/Section1567/Section1823-8066.htm
2. Vestergaard, M.; Kerman, K.; Tamiya, E. The study of Alzheimer's disease biomrkers: current and future prospects of nanosensor technology. Nanobiotechnology, 2006, 2, 5-16.
3. Haass C. Take five-BACE and the c-secretase quartet conduct Alzheimer's amyloid b- peptide generation. Eur. Mol. Biol. Org., 2004, 23, 483-488.
4. LaFerla, F.M.; Green, K.N.; Oddo, S. Intracellular amyloid-in Alzheimer's disease. Nat. Rev. Neurosci., 2007, 8, 499-509.
5. Chauhan, N.B. Membrane dynamics, cholesterol homeostasis, and Alzheimer's disease. J. Lipid Res., 2003, 44, 2019-2029.
6. Verdile, G.; Fuller, S.; Atwood, C.S.; Laws, S.M.; Gandy, S.E.; Martins, R.N. The role of amyloid beta in Alzheimer's disease: Still a cause of everything or the only one who got caught? Pharmacol. Res., 2004, 50, 397-409.
7. Arispe, N.; Diaz, J.C.; Simakova, O. Prospects pf treating Alzheimer's disease with Aβ channel blockers. Biochim. Biophys. Acta, 2007, 1768, 1952-1965.
8. Stine Jr. W.B.; Dahigren K.N.; Krafft G.A.; LaDu, M.J. In vitro characterisation of conditions for amyloid- peptide oligomerisation and fibrilogenesis. J. Biol. Chem., 2003, 278, 11612-11618.
9. Nunan, J.; Small, D.H. Regulation of APP cleavage by α-, β- and γ-secretases. FEBS Lett., 2000, 483, 6-10.
10. Shen, C.L.; Murphy, R.M. Solvent effects on self-assembled β-amyloid peptide. Biophys. J. 1995, 69, 640-651.
11. Lippa, C.F.; Nee, L.E.; Mori, H.; George-Hyslop, P. Amyloid-beta-42 precedes other pathology in familial Alzheimer's disease. Lancet, 1998, 352, 1117-1118.
12. Asami-Odaka, A.; Ishibashi, Y.; Kikuchi, T.; Kitada, C.; Suzuki, N. Long amyloid. beta.-protein secreted from wild-type human neuroblastoma IMR-32 cells. Biochemistry, 1995, 34, 10272.
13. Jarrett, J.; Berger, E.; Lansbury, P. The carboxy terminus of the beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease. Biochemistry, 1993, 32, 4693-4697.
14. Padrick, S.B., Miranker, A.D. Islet amyloid: phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis. Biochemistry, 2002, 41, 4694-4703.
15. Slusky, V., Tamada, J.A.; Klibanov, A.M.; R. Langer, R. Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces. Proc. Natl. Acad. Sci. USA, 1991, 88, 9377-9381.
16. Hardy, J.A.; Higgins, G.A. Alzheimer's disease: the amyloid cascade hypothesis. Science, 2006, 256, 184-185.
17. Lesne, S.; Toh, M.T.; Kotlinek, L.; Kayed, R.; Glabe, C.G.; Yang, A. A specific amyloid-b protein assembly in the brain impairs memory. Nature, 2006, 440, 353-357.
18. Walsh, D.M.; Klyubin, I.; Fadeeva, J.V.; Cullen, W.K.; Anwyl, R.; Wolfe, M.S.; Rowan, M.J.; Selkoe, D.J. Naturally secreted oligomers of amyloid b protein potently inhibit hippocampal longterm potentiation in vivo. Nature, 2002, 416, 535-539.
19. Naslund, J.; Harautunian, V.; Mohs, R.; Davis, K.L.; Davies, P.; Greengard, P.; Bauxbaum, J.D. Correlation between elevated levels of amyloid b-peptide in the brain and cognitive decline. J. Am. Med. Assoc., 2000, 283, 1571-1577.
20. Lue, L.F.; Kuo, Y.M.; Roher, A.E.; Brachova, L.; Shen, Y.; Sue, L.; Beach, T.; Kurth, J.H.; Rydel, R.E.; Rogers, J. Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease. Am. J. Pathol., 1999, 155, 853-862.
21. Walsh, D.M.; Townsend, M.; Podlisny, M.B.; Shankar, G.M.; Fadeeva, J.V.; El Agnaf, O.; Hartley, D.M.; Selkoe, D.J. Certain inhibitors of synthetic amyloid -peptide (A) fibrillogenesis block oligomerization of natural A and thereby rescue long-term potentiation. J. Neurosci., 2005, 25, 2455-2462.
22. Zhang, X.Q.; Smith, D.L.; Merlin, A.B.; Engemann, S.; Russel, D.E.; Roark, M.; Washington, S.L.; Maxwell, M.M.; Marsh, J.L.; Thompson, L.M.; Wanker, E.E.; Young, A.B.; Housman, D.E.; Bates, G.P.; Sherman, M.Y.; Kazantsev, A.G. A potent small molecule inhibits polyglutamine aggregation in Huntington's disease neurons and suppresses neurodegeneration in vivo. Proc. Natl. Acad. Sci., USA, 2005, 102, 892-897.
23. Liu, D.; Xu, Y.; Feng, Y.; Liu, H.; Shen, X.; Hen, K.; Ma, J.; Jiang, H. Inhibitor discovery targeting the intermediate structure of beta-amyloid peptide on the conformational transition pathway: implications in the aggregation mechanism of beta-amyloid peptide. Biochemistry, 2006, 45, 10963-10972.
24. Kim, J.R.; Murphy, R.M. Mechanism of accelerated assembly of ß-Amyloid Filaments into Fibrils by KLVFFK6. Biophys. J., 2004, 86, 3194-3203.
25. Gibson, J.J.; Murphy, R.M. Design of peptidyl compounds that affect beta-amyloid aggregation: importance of surface tension and context. Biochemistry, 2005, 44, 8898-8907.
26. Martins, I.C.; Keperstein, I.; Wilkinson, H.; Maes, E.; Vanbrabant, M.; Jonckheere, W.; Van Gelder, P.; Hartman, D.; D'Hooge, R.; De Strooper, B.; Schymkowitz, J.; Rousseau, F. Lipids revert inert Ab amyloid fibrils to neurotoxic protofibrils that affect learning in mice. Eur. Mol. Biol. Org., 2008, 27, 224-233.
27. Vestergaard, M.; Hamada, T.; Takagi, M. Using model membranes for the study of amyloid beta:lipid interactions and neurotoxicity. J. Biotechnol. Bioeng., 2008, 99, 753-763.
28. Murphy, R.M. Kinetics of amyloid formation and membrane interaction with amyloidogenic proteins. Biochim. Biophys. Acta, 2007, 1768, 1923-1934.
29. Bitan, G.; Kirkitadze, M.D.; Lomakin, A.; Vollers, S.S.; Benedek, G.B.; Teplow, D.B. Amyloid beta-protein (Abeta) assembly: AB 40 and Abeta 42 oligomerise through distinct pathways. Proc. Natl. Acad. Sci. USA, 2003, 100, 330-335.
30. Nichols, M.R.; Moss, M.A.; Dana Kim Reed, D.K.; Cratic-McDaniel, S.; Hoh, J.H.; Rosenberry, T.L. Amyloid- protofibrils differ from amyloid- aggregates induced in dilute hexafluoroisopropanol in stability and morphology. J. Biol. Chem., 2005, 280, 2471-2480.
31. Matsuzaki, K. Physicochemical interactions of amyloid β-peptide with lipid bilayers. Biochim. Biophys. Acta, 2007, 1768, 1935-1942.
32. Murphy, R.M.; Pallitto, M.M. Probing the kinetics of beta-amyliod self-association. J. Struct. Biol., 2000, 130, 109-122.
33. Snyder, S.W.; Ladror, U.S.; Wade, W.S.; Wang, G.T.; Barrett, L.W.; Matayoshi, E.D.; Huffaker, H.J.; Krafft, G.A.; Holzman, T.F. Amyloid-beta aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lengths. Biophys. J., 1994, 67, 1216-1228.
34. Söderberg, L.; Dahlqvist, C.; Kakuyama, H.; Thyberg, J.; Ito, A.; Winblad, B.; Näslund, J.; Tjernberg, L.O. Collagenous Alzheimer amyloid plaque component assembles amyloid fibrils into protease resistant aggregates. FEBS J., 2005, 272, 2231-2236.
35. Necula, M.; Kayed, R.; Milton, S.; Glabe, C.G. Small Molecule Inhibitors of Aggregation Indicate That amyloid oligomerization and fibrillization pathways are independent and distinct. J. Biol. Chem., 2007, 282, 10311-10324.
36. Stege, G.J.J.; Renkawek, K.; Overkamp, P.S.G.; Verschuure, P.; van Rijk, A.F.; Reijnen- Aalbers, A.; Boelens, W.C.; Bosman, G.J.; de Jong, W.W. The molecular chaperone alphaB- crystallin enhances amyloid beta neurotoxicity. Biochem. Biophys. Res. Commun., 1999, 262, 152-156.
37. Vassar, P.S.; Culling, C.F.A. Fluorescent stains, with special reference to amyloid and connective tissues. Arch. Pathol., 1959, 68, 487-498.
38. Kelenyi G. Thioflavin S fluorescent and Congo red anisotropic stainings in the histologic demonstration of amyloid. Acta Neuropathol., 1967, 7, 336-348.
39. Levine-III, H. Thioflavine T interaction with synthetic Alzheimer's disease {beta}-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci., 1993, 2, 404-410.
40. Krebs, M.R.H.; Bromley, E.H.C.; Donald, M.A. The binding of thioflavin-T to amyloid fibrils: localization and implications. J. Struct. Biol., 2005, I, 20-37.
41. Khurana, R.; Coleman, C.; Ionescu-Zanetti, C.; Carter, S.A., Krishn, V.; Grover, R.K.; Royd, R.; Singh, S. Mechanism of thioflavit T binding to amyloid fibrils. J. Struct. Biol., 2005, 151, 229-238.
42. Nichols, M.R.; Moss, M.A.; Reed, D.K.; Cratic-McDaniel, S.; Hoh, J.H.; Rosenberry, T.L. Amyloid-b protofibrils differ from amyloid-b aggregates induced in dilute hexafluoroisopropanol in stability and morphology. J. Biol. Chem., 2005, 80, 2471-2480.
43. Luo, Y.; Smith, J.V.; Paramasivam, V.; Burdick, A.; Curry, K.J.; Buford, J.P.; Khan, I.; Netze, W.J.; Xu, H.; Butko, O.P. Inhibition of amyloid-?? aggregation and caspase-3 activation by the Ginkgo biloba extract Egb761. Proc. Natl. Acad. Sci. USA, 2002, 99, 12197-12202.
44. Tomiyama, T.; Shoji, A.; Kataoka, K.; Suwa, Y.; Asano, S.; Kaneko, H.; Endo, N. Inhibition of amyloid beta protein aggregation and neurotoxicity by rifampicin. Its possible function as a hydroxyl radical scavenger. J. Biol. Chem., 1996, 271(12), 6839-6844.
45. Kumar, S.S.; Quiju, D.; Lixia, Y.; Chan, W-S.; Kum, W-F.; Chenli, K.; Song, Y.; Huang, J- D.; Klein, W.L. Neurochem. Int., 2008, 52, 741.
46. Ono, K.; Hasegawa, K.; Naiki, H.; Yamada, M. J. Curcumin has potent anti-amyloidogenic effects for Alzheimer's -amyloid fibrils in vitro. Neurosci. Res., 2004, 75, 742-750.
47. Nilsson, M.R. Techniques to study amyloid fibril formation in vitro. Methods, 2004, 34, 151-160.
48. Bourhim, M.; Kruzel, M.; Nicoter, T.S. Thioflavin T as a fluorescent reporter for β aggregation. J. Neurosci. Methods, 2007, 160, 264.
49. Hartley, D.M.; Walsh, D.M.; Ye, C.P.; Diehl, T.; Vasquez, S.; Vassilev, P.M.; Teplow, D.JB.; Selkoe, D.J. Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 1999, 19, 8876-8884.
50. Nichols, M.R.; Moss, M.A.; Reed, D.K.; Cratic-McDaniei, S.; Hoh, J.H.; Rosenberry, T.L. Amyloid- protofibrils differ from Amyloidaggregates induced in dilute hexafluoroisopropanol in stability and morphology. J. Biol. Chem., 2005, 280, 2471-2480.
51. Williams, A.D.; Sega, M.; Chen, M.L.; Kheterpal, I.; Geva, M.; Berthelier, V.; Kaleta, D.T.; Cook, K.D.; Wetzel, R. Structural properties of A{beta} protofibrils stabilized by a small molecule. Proc. Natl. Acad. Sci. USA, 2005, 102, 7115-7120.
52. Liedberg, B.; Nylander, C.; Lundstr6m, I. Surface plasmon resonance for gas detection and biosensing. Sens. Actuators, 1983, 4, 299-304.
53. Gordon, J.G.; Ernst, S. Surface plasmons as a probe of the electrochemical interface. Surf. Sci., 1998, 101, 499-506.
54. Schuck, P. Use of surface plasmon resonance to probe the equilibrium and dynamic aspects of interactions between biological macromolecules. Annu. Rev. Biophys. Biomol. Struct., 1997, 26, 541-566.
55. Karlsson, R.J. SPR for molecular interaction analysis: a review of emering application areas. J. Mol. Recognit., 2004, 17, 151-161.
56. Win, M.N.; Klein, J.S.; Smolke, C.D. RNA aptamers to the benzylisoquinoline alkaloid codeine and the rapid characterization of their binding properties using surface plasmon resonance. Nucleic Acids Res., 2006, 34, 5670-5682.
57. Tombelli, S.; Minunni, M.; Luzi, E.; Mascini, M. Aptamer-based biosensors for the detection of HIV-1 Tat protein. Bioelectrochem., 2005, 67, 135-141.
58. Misono, T.S.; Kumar, P.K.R. Selection of RNA aptamers against human influenza virus hemagglutinin using surface plasmon resonance. Anal. Biochem., 2005, 342, 312-317.
59. Murphy, M.B.; Fuller, S.T.; Richardson, P.M.; Doyle, S.A. An improved method for the in vitro evolution of aptamers and applications in protein detection and purification. Nucleic Acids Res., 2003, 31, e110-e110.
60. Li, Y.; Lee, H.J.; Corn, R.M. Fabrication and characterization of RNA aptamer microarrays for the study of protein-aptamer interactions with SPR imaging. Nucleic Acids Res., 2006, 34, 6416-6424.
61. Hasegawa, K.; Ono, M.; Yamada, M.; Naiki, H. Kinetic modeling and determination of reaction constants of Alzheimer's beta-amyloid fibril extension and dissociation using surface plasmon resonance. Biochemistry, 2002, 41, 13489-13498.
62. Cannon, M.J.; Williams, A.D.; Wetzel, R.; Myszka, D.G. Kinetic analysis of beta- amyloid fibril elongation. Anal. Biochem., 2004, 328, 67-75.
63. Ariga, T.; Kobayashi, K.; Hasegawa, A.; Kiso, M.; Ishida, H.; Miyatake, T. Characterization of high-affinity binding between gangliosides and amyloid β-protein. Arch. Biochem. Biophys., 2001, 388, 225-230.
64. Ryu, J.; Joung, H-A.; Kim, M-G.; Chan Beum Park, C.B. Surface plasmon resonance analysis of Alzheimer's β-amyloid aggregation on a solid surface: from monomers to fully- grown fibrils. Anal. Chem., 2008, 80, 2400-2407.
65. Nehl, C.L.; Hafner, J. H. J. Shape-dependent resonant properties of gold nanoparticles. Mater. Chem., 2008, 18, 2415-2419.
66. Murray, W.A.; William L.; Barnes, W.L. Plasmonic materials. Adv. Mater., 2007, 19, 3771-3782.
67. Haes, A.J.; Van Duyne, R.P. A nanoscale optical biosensor: sensitivity and selectivity of an approach based on the localized surface plasmon resonance spectroscopy of triangular silver nanoparticles. J. Am. Chem. Soc., 2002, 124, 10596-10604.
68. Kim, D-K.; Kerman, K.; Yamamura, S.; Young-Soo Kwon, Y-S.; Takamura, Y.; Tamiya, E. Label-free optical detection of protein antibody-antigen interaction on Au cupped porous anodic alumina layer chip. Jpn. J. Appl. Phys., 2008, 47, 1351-1354.
69. Nath, N.; Chilkoti, A. A colorimetric gold nanoparticle sensor to interrogate biomolecular interactions in real time on a surface. Anal. Chem., 2002, 74, 504-509.
70. Nath, N.; Chilkoti, A. Label-free biosensing by surface plasmon resonance of nanoparticles on glass: optimization of nanoparticle size. Anal. Chem., 2004, 76, 5370-5378.
71. Fujiwara, K.; Watarai, H.; Itoh, H.; Nakahama, E.; Ogawa, N. Measurement of antibody binding to protein immobilized on gold nanoparticles by localized surface plasmon spectroscopy. Anal. Bioanal. Chem., 2006, 386, 639-644.
72. Ruach-Nir, I.; Bendikov, T.A.; Doron-Mor, I.; Barkay, Z.; Vaskevich, A.; Rubinstein, I. Silica-stabilized gold island films for transmission localized surface plasmon sensing. J. Am. Chem. Soc., 2007, 129, 84-92.
73. Vestergaard, M.; Kerman, K.; Kim, D-K.; Ha, M.H. Detection of Alzheimer's tau protein using localised surface plasmon resonance-based immunochip. Talanta, 2008, 4, 753-742.
74. Kato, K.; Barsukov, L.Y.; Derrick, J.P.; Kim, H.; Tanaka, R.; Yoshimo, A.; Shiraishi, M.; Shimada, I.; Arata, Y. Model for the complex between protein G and an antibody Fc fragment in solution. Structure, 1995, 3, 79-85.
75. Hu, Y.Y.; He, S.S.; Wang, X.; Duan, Q.H.; Grundke-Iqbal, I.; Iqbal, K.; Wang, J. Levels of nonphosphorylated and phosphorylated tau in cerebrospinal fluid of Alzheimer's disease patients: An ultrasensitive bienzyme-substrate- recycle enzyme-linked immunosorbent assay. Am. J. Pathol., 2002, 160, 1269-1278.
76. Vestergaard, M.; Tamiya, E. A rapid sample pretreatment protocol: improved sensitivity in the detection of a low-abundant serum biomarker for prostate cancer. Anal. Sci., 2007, 23, 1443-1446.
77. Haes, A.J.; Hal, P.W.; Chang, L.; Klein, W.L.; Van Duyne, R.P. A localised surface plasmon resonance biosensor: first steps toward an assay for Alzheimer's disease. Nano Lett., 2004, 4, 1029-1034.
78. Haes, A.J.; Chang, L.; Klein, W.L.; Van Duyne, R.P. Detection of a biomarker for Alzheimer's disease from synthetic and clinical samples using a nanoscale optical biosensor. J. Am. Chem. Soc., 2005, 127, 2264-2271.
79. Georganopoulou, D.G.; Chang, L.; Nam, J-M.; Thaxton, C.S.; Mufson, E.J.; Klein, W.L.; Mirkin, C.A. Nanoparticle- based detection in cerebrospinal fluid of a soluble pathogenic biomarker for Alzheimer's disease. Proc. Natl. Acad. Sci. USA, 2005, 102, 2273-2276.
80. Vestergaard, M.; Kerman, K.; Saito, M.; Nagatani, N.; Takamura, Y.; Tamiya, E. A rapid label-free electrochemical detection and kinetic study of Alzheimer's amyloid beta aggregation. J. Am. Chem. Soc., 2005, 127, 11892-11893.
81. Armstrong, F. A. In: Wilson, G. S.; Ed. Bioelectrochem., 2002, vol. 9. Wiley-VCH, Weinheim, 11-29.
82. Brabec, V.; Schindlerova, I. 434 - Electrochemical behaviour of proteins at graphite electrodes: Part III. The effect of protein adsorption. Bioelectrochem. Bioenerg., 1981, 8, 451-458.
83. Brabec, V.; Mornstein, V. Electrochemical behaviour of proteins at graphite electrodes : II. Electrooxidation of amino acids. Biophys. Chem., 1980, 12, 159-165.
84. Tomschik, M.; Havran, L.; Palecek, E.; Heyrovsky, M. The presodium catalysis of electroreduction of hydrogen ions on mercury electrodes by metallothionein. An investigation by constant current derivative stripping chronopotentiometry. Electroanalysis, 2000, 12, 274.
85. Reynaud, J.A.; Malfoy, B.; Bere, A. 359 - The electrochemical oxidation of three proteins: RNAase A, bovine serum albumin and concanavalin A at solid electrodes. J. Electroanal. Chem., 1980, 116, 595-606.
86. Reynolds Jr., N. C.; Kissela, B. M.; Fleming, L. H. The voltammetry of neuropeptides containing L-tyrosine. Electroanalysis, 1995, 7, 1177-1181.
87. Cai, X.; Rivas, G.; Farias, P.A.M.; Shiraishi, H.; Wang, J.; Palecek, E. Potentiometric stripping analysis of biologically important bioactive peptides at carbon electrodes. Anal. Chim. Acta, 1996, 332, 49-57.
88. Kerman, K.; Vestergaard, M.; Chikae, M.; Yamamura, S.; Tamiya, E. Label-free electrochemical detection of phosphorylated and nonphosphorylated forms of peptides based on tyrosine oxidation. Electrochem. Commun., 2007, 9, 976-980.
89. Kerman, K.; Vestergaard, M.; Tamiya, E. Label-free electrical sensing of small-molecule inhibition on tyrosine phosphorylation. Anal. Chem., 2007, 79, 6881-6885.
90. Vestergaard, M.; Kerman, K.; Tamiya, E. An overview of label-free electrochemical protein sensors. Sensors, 2007, 7, 3442-3458.
91. Herzog, G.; Arrigan, D.W.M. Electrochemical strategies for label-free detection of amino acids, peptides and proteins. Analyst, 2007, 132, 615-632.
92. El-Agnaf, O.M.A.; Mahil, D.S.; Patel, B.P.; Austen, B.M. Oligomerization and toxicity of b- amyloid-42 implicated in Alzheimer's disease. Biochem. Biophys. Res. Commun., 2000, 273, 1003-1007.
93. Masařík, M.; Stobiecka, A.; Kizek, R.; Jelen, F.; Pechan, Z.; Hoyer, W.; Jovin, T.; Subramaniam, V.; Paleček, E. Sensitive electrochemical detection of native and aggregated alpha-synuclein protein involved in Parkinson's disease. Electroanalysis, 2004, 16, 1172-1181.
94. Yanagisawa K. Role of gangliosides in Alzheimer'S disease. Biochim. Biophys. Acta, 2007, 1768, 1943-1951.
95. Matsuzaki K. Physicochemical interactions of amyloid β-peptide with lipid bilayers. Biochim. Biophys. Acta, 2007, 1768, 1935-1942.
96. Chikae, M.; Fukuda, T.; Kerman, K.; Idegami, K.; Miura,Y.; Tamiya, E. Amyloid-β detection with saccharide immobilized gold nanoparticle on carbon electrode Bioelectrochemistry, 2008, 74, 118-123.
97. Vestergaard, C.M.; Hamada, T.; Saito, M.; Yajima, Y.; Kudou, M.; Tamiya, E.; Takagi, M. The Detection of Alzheimer's amyloid beta aggregation by capturing molecular trails of individual assemblies. Biochem. Biophys. Res. Comm., 2008, 377, 725-728.
98. Berne, B.J.; Pecola., R. Dynamic light scattering, John Wiley and sons, NY, 1976.
99. Murphy, R.M.; Yarmush, M.L.; Colton, C.K. Determining molecular weight distributions of antigen-antibody complexes by quasielastic light scattering. Biopolymers, 1991, 11, 1289-1295.
100. Sharma, P.; Rajalingam, D.; Krishnaswamy, T.; Kumar, S.; Singh , S. A light scattering study of the interaction of fibroblast growth factor (FGF) with its receptor. Biophys. J. 2008, 74, L71-L73.
101. Araki, S.; Nakai, T.; Hizume, K.; Takesu, K.; Yoshikawa, K. Hydrodynamic radius of circular DNA is larger than that of linear DNA. Chem. Phys. Lett., 2006, 418, 255-59.
102. Liu Ru, L.; Wei, Q.; Rongxin, S.; Yubin, Z.; Fengmin, J.; Zhimin, H. Dissolution and enzymatic hydrolysis of casein micelles studied by dynamic light scattering. Frontiers Chem. Eng., 2007, 1, 123.
103. Yong, W.; Lomakin, A.; Kirkitadze, M.D.; Teplow, D. B.; Chen, SH. Structure determination of micelle-like intermediates in amyloid beta-protein fibril assembly by using small angle neutron scattering. Proc. Natl. Acad. Sci. USA, 2002, 99, 150-154.
104. Carrotta, R.; Manno, M.; Bulone, D.; Vincenzo Martorana, and Pier Luigi San Biagio. P. J. Protofibril formation of amyloid β-protein at low pH via a non-cooperative elongation mechanism. Biol. Chem., 2005, 280, 30001-30008.
105. Lomakin, A.; Chung, D.S.; Benedek, G.B., Kirschner, D.A. On the Nucleation and Growth of Amyloid beta-Protein Fibrils: Detection of Nuclei and Quantitation of Rate Constants. Proc. Natl. Acad. Sci. USA, 1996, 96, 1125-1129.
106. Matsumoto, M.; Sakaguchi, T.; Kimura, H.; Doi, M.; Minagawa, K.; Matsuzawa, Y.; Yoshikawa, K. Direct observation of Brownian motion of macromolecules by fluoresence microscope. J. Polym. Sci. B: Polym. Phys., 1992, 30, 799-783.
107. Balbach, J.J.; Petkova, A.T.; Oyler, N.A.; Antzutkin, O.N.; Gordon, D.J.; Meredith, S.C.; Robert Tycko, R. Supramolecular structure in full-length Alzheimer's beta-amyloid fibrils: evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance. Biophys. J., 2002, 83, 1205-1216.
108. Kelly, J.W. Amyloid fibril formation and protein misassembly: A structural quest for insights into amyloid and prion diseases. Structure, 1997, 5, 595-600.
109. Malinchik, S.B.; Inouye, H.; Szumowski, K.E.; Kirschner, D.A. Structural analysis of Alzheimer's beta(1-40) amyloid: protofilament assembly of tubular fibrils. Biophys. J., 1998, 74, 537-545.
110. Kelly, S.M.; Price, N.C. The use of circular dichroism in the investigation of protein structure and function. Curr. Protein Peptide Sci., 2000, 1, 349-384.
111. McClelland, D.A.; McLaughlin, S.H.; Freedman, R.B.; Price, N.C. The refolding of hen egg white riboflavin-binding protein: effect of protein disulphide isomerase on the reoxidation of the reduced protein. Biochem. J., 1995, 311, 133-137.
112. Xia, J.; Dubin, P.L.; Kokufuta, E.; Havel, H.; Muhoberac, B.B. Light scattering, CD, and ligand binding studies of ferrihemoglobin-polyelectrolyte complexes. Bioplolymers, 1999, 50, 153-161.
113. Zsila, F.; Matsunaga, H.; Bikadi, Z.; Haginaka, J. Multiple ligand-binding properties of the lipocalin member chicken alpha(1)-acid glycoprotein studied by circular dichroism and electronic absorption spectroscopy: The essential role of the conserved tryptophan residue. Biochim. Biophys. Acta, 2006, 1760, 1248-1273.
114. Izumikawa, N.; Nishikori, S.; Vestergaard, M.; Hamada, T.; Hagihara, Y.; Yumoto, N.; Shiraki, K.; Takagi, M. Effect of phospholipids on conformational structure of bovine pancreatic trypsin inhibitor (BPTI) and its thermolabile mutants. Biopolymers 2008, Biopolymers, 89, 873-880.
115. Nishikori, S.; Shiraki, K.; Fujiwara, S.; Imanaka, T.; Takagi, M. Unfolding mechanism of a hyperthermophilic protein O(6)-methylguanine-DNA methyltransferase. Biophys. Chem., 2005, 116, 97-104.
116. Kelly, S.M.; Price, N.C. The application of circular dichroism to studies of protein folding and unfolding. Biochim. Phys. Acta, 1997, 1338, 161-185.
117. Pallares, I.; Vendrell, J.; Avilles, F.X; Ventura, S. Amyloid fibril formation by a partially structured intermediate state of alphachymotrypsin. J. Mol. Biol., 2004, 342, 321-331.
118. Yoshiike, Y.; Tanemura, K.; Ohoshi Murayama, O.; Akagi, T.; Murayama, M.; Shinji, S.; Sun, X.; Anaka, N.; Takashima, A. new insights on how metals disrupt amyloid -aggregation and their effects on amyloid- cytotoxicity. J. Biol. Chem., 2001, 276, 32293-32299.
119. Gupta, V.B.; Indi, S.S.; Rao. K.S.J. Studies on the role of amino acid stereospecificity in amyloid beta aggregation. J. Mol. Neurosci., 2008, 34, 35-43.
120. Clark, D.T.; Jones, G.R. Extended circular dichroism measurements using synchrotron radiation show that the assembly of clathrin coats requires no change in secondary structure. Biochemistry, 1999, 38, 10457-10462.
121. Chaffotte, A.F.; Guillou, Y.; Goldberg, M.E. Kinetic resolution of peptide bond and side chain far-UV circular dichroism during the folding of hen egg white lysozyme. Biochemistry, 1992, 31, 9694-96702.
122. Schabert, F.A.; Henn, C.; Engel, A. Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy. Science, 1995, 268, 92-94.
123. Shao, Z.; Mou, J.; Czajkowsky, D.M.; Yang, J.; Yuan, J.-Y. Biological atomic force microscopy: what is achieved and what is needed. Adv. Phys., 1996, 45, 1-86.
124. Branchard, S. Atomic force microscopy. Chem. Educ., 1996, 1, 1-8.
125. Hansma, H.G.; Revenko, I.; Kim, K.; Laney, D.E. Atomic force microscopy of long and short double-stranded, single-stranded and triple-stranded nucleic acids. Nucleic Acids Res., 1996, 24,713-720.
126. Saito, M.; Takamura, Y.; Tamiya, E. Nanoscale time-lapse AFM imaging in solution for DNA aggregation. NanoBiotechnology, 2005, 1, 361.
127. Bezanilla, M.; Drake, B.; Nudler, E.; Kashlev, M.; Hansma, P.; Hansma, H.G. Motion and enzymatic degradation of DNA in the atomic force microscope. Biophys. J., 1994, 67, 2454-2459.
128. Florin, E.-L., Vincent, T.M.; Gaub, H.E. Adhesion forces between individual ligand-receptor pairs. Science, 1994, 264, 415-417.
129. Viani, M.B.; Pietrasanta, L.I.; Thompson, J.B.; Chand, A.; Gebeshuber, I.C.; Kindt, J.H.; Richter, M.; Hansma, H.G.; Hansma, P.K. Probing protein-protein interactions in real time. Nat. Struct. Biol., 2000, 7, 644-647.
130. Thomson, N.H.; Fritz, M.; Radmacher, M.; Cleveland, J.P.; Schmidt, C.F.; Hansma, P.K. Protein tracking and detection of protein motion using atomic force microscopy. Biophys. J., 1996, 70, 2421-2431.
131. Iwabuchi, S.; Mori, T.; Ogawa, K.; Sato, K.; Saito, M.; Morita, Y.; Ushiki, T.; Tamiya, E. Atomic force microscope-based dissection of human metaphase chromosomes and high resolutional imaging by carbon nanotube tip. Arch. Histol. Cytol., 2002, 65, 473-479.
132. Prabhu, A.; Lin, H.; Thimm, J.; Lal, R. Imaging real-time aggregation of amyloid beta (1-42) by atomic force microscopy. Peptides, 2002, 23, 1265.
133. 2+- sensitive channel. J. Biol. Chem., 1998, 273, 13379-13382.
134. Lin, H.; Bhatia, R.; Lal, R. Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology. FEBS J., 2001, 15, 2433-2444.
135. McAllister, C.; Karymov, M.A.; Kawano, Y.; Lushnikov, A.Y.; Mikheikin, A; Uversky, V.N.; Lyubchenko, Y.L. Protein Interactions and Misfolding Analyzed by AFM Force Spectroscopy. J. Mol. Biol., 2005, 354, 1028.
136. Taniguchi, N. On the basic concept of 'nano-technology, Proc. Int. Conf. Prod. Eng., Part II, Japan Society of Precision Engineering, Tokyo, Japan, 1974;
137. Bullchman, P.; Ed. Electroanalysis based on nanomaterials (editorial). TrAc Trends Anal. Chem., 2008, vol. 27, p. 567.
138. Kroto, H.W.; Heath, J.R.; O'Brien, S.C.; Curl, R.F.; Malley, R.E. C60: buckminsterfullerene. Nature, 1985, 318, 62-63.
139. Iijima, S. Helical microtubules of graphitic carbon. Nature, 1991, 354, 56-58.
140. Fojta, M.; Palecek, E. Supercoiled DNA-modified mercury electrode: A highly sensitive tool for the detection of DNA damage. Anal. Chim. Acta, 1997, 342, 1-12.
141. Wang, J. Electrochemical nucleic acid biosensors. Anal. Chim. Acta, 2002, 469, 63-71.
142. Gauglitz, G.; Direct optical sensors: principles and selected applications. Anal. Bioanal. Chem., 2005, 381, 141-155.
143. Huang, H.; Chen, Y. Label-free reading of microarray-based proteins with high throughput surface plasmon resonance imaging. Biosens Bioelectron., 2006, 22, 644-648.
144. Banks, C.E.; Crossley, A.; Salter, C.; Wilkins, S.J.; Compton, R. G. Carbon Nnnotubes contain metal impurities which are responsible for the electrocatalysis seen at some nanotube-modified electrodes. Angew. Chem. Int. Ed. Engl., 2006, 45, 2533-2537.
145. Okuno, J.; Maehashi, K.; Matsumoto, K.; Kerman, K.; Takamura, Y.; Tamiya, E. Single- walled carbon nanotube-arrayed microelectrode chip for electrochemical analysis. Electrochem. Commun., 2007, 9, 13-18.
146. Okuno, J.; Maehashi, K.; Kerman, K.; Takamura, Y.; Matsumoto, K.; Tamiya, E. Label-free immunosensor for prostate-specific antigen based on single-walled carbon nanotube array- modified microelectrodes. Biosens. Bioelectron., 2007, 22, 2377-2381.
147. Kerman, K.; Kobayashi, M.; Tamiya, E. Recent trends in electrochemical DNA biosensor technology. Measure. Sci. Technol., 2004, 15, R1-R11.
148. Ozsoz, M.; Erdem, A.; Kerman, K.; Ozkan, D.; Tugrul, B.; Topcuoglu, N.; Ekren, H.; Taylan, M. Electrochemical genosensor based on Ccolloidal gold nanoparticles for the detection of factor V leiden mutation using disposable pencil graphite electrodes. Anal. Chem., 2003, 75, 2181-2187.
149. Kerman, K.; Saito, M.; Morita, Y.; Takamura, Y.; Ozsoz, M.; Tamiya, E. Electrochemical coding of single nucleotide polymorphisms by monobase modified gold nanoparticles. Anal. Chem., 2004, 76, 1877-1884.
150. Merkoc, A.; Alegret, S. Toward nanoanalytical chemistry. Case of nanomaterial integration into (bio)sensing systems. Contrib. Sci., 2005, 3, 57-66.
151. Chikae, M.; Idegami, K.; Kerman, K.; Nagatani, N.; Ishikiwa, M.; Takamura, Y.; Tamiya, E. Direct fabrication of catalytic metal nanoparticles onto the surface of a screen-printed carbon electrode. Electrochem. Commun., 2006, 8, 1375-1380.
152. Siegmund, T.; Paulke, B.-R.; Schimiedel, H.; Bordag, N.; Hoffmann, A.; Harkany, T.; Tanila, H.; Kacza, J.; Hartig, W. thioflavins released from nanoparticles target fibrillar amyloid β in the hippocampus of APP/PS1 transgenic mice. Int. J. Dev. Neurosci., 2006, 24, 195-201.
153. Hafner, J.H.; Cheung, C.-L.; Woolley, A.T.; Lieber, C.M. Structural and functional imaging with carbon nanotube AFM probes. Prog. Biophy. Mol. Biol., 2001, 77, 73-110.
154. Koh, C.J.; Lee, M. Structural analysis of amyloid aggregates by multifunctional fluorescence nanoscopy. Curr. Appl. Phys., 2006, 6S1, e257-e260.
155. Kerman, K.; Morita, Y.; Takamura, Y.; Ozsoz, M.; Tamiya, E. DNA-directed attachment of carbon nanotubes for the enhanced electrochemical label-free detection of DNA hybridization. Electroanalysis, 2004, 16, 1667-1672.
156. Katz, E.; Willner, I. Integrated nanoparticle-biomolecule hybrid systems: synthesis properties and applications. Angew. Chem., 2004, 43, 6042-6108.