Abstract
This chapter details the physical theoretical concepts and relevant background knowledge for the SPM techniques, alongside others such as DLS. Current understanding of the nanostructure of the amyloid peptide which has been the focus of this work, Aβ, is also detailed, gathering together information from a variety of experimental techniques. It is the aim of this chapter, and the one that follows it to provide a solid understanding of the work conducted within this thesis, and its relevance to Alzheimer’s disease and the aggregation of Aβ.
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References
Binnig, G., Quate, C. F., & Gerber, C. (1986). Atomic force microscope. Physical Review Letters, 56, 930–933.
Binnig, G., & Rohrer, H. (1982). Scanning tunneling microscopy. Helvetica Physica Acta, 55, 726–735.
Binnig, G., Rohrer, H., Gerber, C., & Weibel, E. (1982). Tunneling through a controllable vacuum gap. Applied Physics Letters, 40, 178–180.
Jandt, K. D. (2001). Atomic force microscopy of biomaterials surfaces and interfaces. Surface Science, 491, 303–332.
Dinelli, F., Biswas, S. K., Briggs, G. A. D., & Kolosov, O. V. (2000). Measurements of stiff-material compliance on the nanoscale using ultrasonic force microscopy. Physical Review B, 61, 13995–14006.
Dinelli, F., et al. (2000). Mapping surface elastic properties of stiff and compliant materials on the nanoscale using ultrasonic force microscopy. Philosophical Magazine A Physics of Condensed Matter Structure Defects and Mechanical Properties, 80, 2299–2323.
Dinelli, F., Assender, H. E., Takeda, N., Briggs, G. A. D., & Kolosov, O. V. (1999). Elastic mapping of heterogeneous nanostructures with ultrasonic force microscopy (UFM). Surface and Interface Analysis, 27, 562–567.
Dazzi, A., et al. (2012). AFM-IR: Combining atomic force microscopy and infrared spectroscopy for nanoscale chemical characterization. Applied Spectroscopy, 66, 1365–1384.
Dazzi, A., Prazeres, R., Glotin, E., & Ortega, J. M. (2005). Local infrared microspectroscopy with subwavelength spatial resolution with an atomic force microscope tip used as a photothermal sensor. Optics Letters, 30, 2388–2390.
Marcott, C., et al. (2012). Nanoscale IR spectroscopy: AFM-IR—A new technique. Spectroscopy, 27, 60–65.
Tovee, P. D., & Kolosov, O. V. (2013). Mapping nanoscale thermal transfer in-liquid environment-immersion scanning thermal microscopy. Nanotechnology, 24.
Tovee, P. D., et al. (2014). Nanoscale resolution scanning thermal microscopy using carbon nanotube tipped thermal probes. Physical Chemistry Chemical Physics, 16, 1174–1181.
Tovee, P., Pumarol, M., Zeze, D., Kjoller, K., & Kolosov, O. (2012). Nanoscale spatial resolution probes for scanning thermal microscopy of solid state materials. Journal of Applied Physics, 112.
Gandyra, D., Walheim, S., Gorb, S., Barthlott, W., & Schimmel, T. (2015). The capillary adhesion technique: A versatile method for determining the liquid adhesion force and sample stiffness. Beilstein Journal of Nanotechnology, 6, 11–18.
Weisenhorn, A. L., Hansma, P. K., Albrecht, T. R., & Quate, C. F. (1989). Forces in atomic force microscopy in air and water. Applied Physics Letters, 54, 2651–2653.
Baro, A. M. R. R. G. (Eds.). (2012). Wiley-VCH.
DoITPoMS. (2013). Teaching and learning package. University of Cambridge. http://www.doitpoms.ac.uk/tlplib/afm/tip_surface_interaction.php. Accessed February 24, 2015.
Bonnell, D. (2001). Scanning probe microscopy and spectroscopy: Theory, techniques, and applications. New York, USA: Wiley-Blackwell.
Eaton, P. W. P. (2010). Atomic force microscopy. Oxford: Oxford University Press.
Kolosov, O. V., & Yamanaka, K. (1993). Nonlinear detection of ultrasonic vibrations in an atomic force microscope. Japanese Journal of Applied Physics Part 2-Letters, 32, L1095–L1098.
Dinelli, F., Biswas, S. K., Briggs, G. A. D., & Kolosov, O. V. (1997). Ultrasound induced lubricity in microscopic contact. Applied Physics Letters, 71, 1177–1179.
Sader, J. E., Chon, J. W. M., & Mulvaney, P. (1999). Calibration of rectangular atomic force microscope cantilevers. Review of Scientific Instruments, 70, 3967–3969.
Robinson, B. J., Kay, N. D., & Kolosov, O. V. (2013). Nanoscale interfacial interactions of graphene with polar and nonpolar liquids. Langmuir, 29, 7735–7742.
Robinson, B. J., et al. (2014). Nanomechanical mapping of graphene layers and interfaces in suspended graphene nanostructures grown via carbon diffusion. Thin Solid Films, 550, 472–479.
Robinson, B. J., & Kolosov, O. V. (2014). Probing nanoscale graphene-liquid interfacial interactions via ultrasonic force spectroscopy. Nanoscale, 6, 10806–10816.
Bosse, J. L., Tovee, P. D., Huey, B. D., & Kolosov, O. V.(2014). Physical mechanisms of megahertz vibrations and nonlinear detection in ultrasonic force and related microscopies. Journal of Applied Physics, 115.
Chaudhury, M. K., & Owen, M. J. (1993). Adhesion hysteresis and friction. Langmuir, 9, 29–31.
Wei, Z., He, M.-F., & Zhao, Y.-P. (2010). The effects of roughness on adhesion hysteresis. Journal of Adhesion Science and Technology, 24, 1045–1054.
Xiao, Y., & Ma, B. (2015). Abeta(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer’s disease.
Fischer-Cripps, A. C. (2007). Introduction to contact mechanics. New York: Springer.
Johnson, K. L., Kendall, K., & Roberts, A. D. (1971). Surface energy and contact of elastic solids. Proceedings of the Royal Society of London Series A Mathematical and Physical Sciences, 324, 301.
Rabe, U., Janser, K., & Arnold, W. (1996). Vibrations of free and surface-coupled atomic force microscope cantilevers: Theory and experiment. Review of Scientific Instruments, 67, 3281–3293.
Rajakarunanayake, Y. N., & Wickramasinghe, H. K. (1986). Nonlinear photothermal imaging. Applied Physics Letters, 48, 218–220.
Williams, C. C., & Wickramasinghe, H. K. (1986). Scanning thermal profiler. Applied Physics Letters, 49, 1587–1589.
Igeta, M., Inoue, T., Varesi, J., & Majumdar, A. (1999). Thermal expansion and temperature measurement in a microscopic scale by using the atomic force microscope. JSME International Journal Series B Fluids and Thermal Engineering, 42, 723–730.
Majumdar, A., Carrejo, J. P., & Lai, J. (1993). Thermal imaging using the atomic force microscope. Applied Physics Letters, 62, 2501–2503.
Fischer, H. (2005). Quantitative determination of heat conductivities by scanning thermal microscopy. Thermochimica Acta, 425, 69–74.
Lee, J., et al. (2006). Electrical, thermal, and mechanical characterization of silicon microcantilever heaters. Journal of Microelectromechanical Systems, 15, 1644–1655.
Gazit, E. (2002). The “Correctly folded” state of proteins: Is it a metastable state. Angewandte Chemie-International Edition, 41, 257.
Dandurand, J., et al. (2014). Conformational and thermal characterization of a synthetic peptidic fragment inspired from human tropoelastin: Signature of the amyloid fibers. Pathologie Biologie, 62, 100–107.
Blancas-Mejia, L. M., et al. (2014). Kinetic control in protein folding for light chain amyloidosis and the differential effects of somatic mutations. Journal of Molecular Biology, 426, 347–361.
Morel, B., Varela, L., & Conejero-Lara, F. (2010). The thermodynamic stability of amyloid fibrils studied by differential scanning calorimetry. Journal of Physical Chemistry B, 114, 4010–4019.
Ortega, J. M., Glotin, F., & Prazeres, R. (2006). Extension in far-infrared of the CLIO free-electron laser. Infrared Physics & Technology, 49, 133–138.
Dazzi, A., Goumri-Said, S., & Salomon, L. (2004). Theoretical study of an absorbing sample in infrared near-field spectromicroscopy. Optics Communications, 235, 351–360.
Dazzi, A., Prazeres, R., Glotin, F., & Ortega, J. M. (2007). Analysis of nano-chemical mapping performed by an AFM-based (“AFMIR”) acousto-optic technique. Ultramicroscopy, 107, 1194–1200.
Dazzi, A., Prazeres, R., Glotin, F., & Ortega, J. M. (2006). Subwavelength infrared spectromicroscopy using an AFM as a local absorption sensor. Infrared Physics & Technology, 49, 113–121.
Wolkers, W. F., Oldenhof, H., Alberda, M., & Hoekstra, F. A. (1998). A fourier transform infrared microspectroscopy study of sugar glasses: Application to anhydrobiotic higher plant cells. Biochimica Et Biophysica Acta-General Subjects, 1379, 83–96.
Marcott, C., et al. (2013). Nanoscale infrared (IR) spectroscopy and imaging of structural lipids in human stratum corneum using an atomic force microscope to directly detect absorbed light from a tunable IR laser source. Experimental Dermatology, 22, 419–421.
Marcott, C., et al. (2014). Localization of human hair structural lipids using nanoscale infrared spectroscopy and imaging. Applied Spectroscopy, 68, 564–569.
Van Eerdenbrugh, B., Lo, M., Kjoller, K., Marcott, C., & Taylor, L. S. (2012). Nanoscale mid-infrared imaging of phase separation in a drug-polymer blend. Journal of Pharmaceutical Sciences, 101, 2066–2073.
Paschalis, E. P., Betts, F., DiCarlo, E., Mendelsohn, R., & Boskey, A. L. (1997). FTIR microspectroscopic analysis of normal human cortical and trabecular bone. Calcified Tissue International, 61, 480–486.
Paschalis, E. P., Betts, F., DiCarlo, E., Mendelsohn, R., & Boskey, A. L. (1997). FTIR microspectroscopic analysis of human iliac crest biopsies from untreated osteoporotic bone. Calcified Tissue International, 61, 487–492.
Mendelsohn, R., Paschalis, E. P., & Boskey, A. L. (1999). Infrared spectroscopy, microscopy, and microscopic imaging of mineralizing tissues: Spectra-structure correlations from human iliac crest biopsies. Journal of Biomedical Optics, 4, 14–21.
Lasch, P., Boese, M., Pacifico, A., & Diem, M. (2002). FT-IR spectroscopic investigations of single cells on the subcellular level. Vibrational Spectroscopy, 28, 147–157.
Wood, B. R., et al. (1998). FTIR microspectroscopic study of cell types and potential confounding variables in screening for cervical malignancies. Biospectroscopy, 4, 75–91.
Lasch, P., Haensch, W., Lewis, E. N., Kidder, L. H., & Naumann, D. (2002). Characterization of colorectal adenocarcinoma sections by spatially resolved FT-IR microspectroscopy. Applied Spectroscopy, 56, 1–9.
Lasch, P., Haensch, W., Naumann, D., & Diem, M. (2004). Imaging of colorectal adenocarcinoma using FT-IR microspectroscopy and cluster analysis. Biochimica Et Biophysica Acta-Molecular Basis of Disease, 1688, 176–186.
Mordechai, S., et al. (2004). Possible common biomarkers from FTIR microspectroscopy of cervical cancer and melanoma. Journal of Microscopy-Oxford, 215, 86–91.
Müeller, T., et al. (2014). Nanoscale spatially resolved infrared spectra from single microdroplets. Lab on a Chip, 14, 1315–1319.
Pryor, N. E., Moss, M. A., & Hestekin, C. N. (2012). Unraveling the early events of amyloid-beta protein (A beta) aggregation: Techniques for the determination of A beta aggregate size. International Journal of Molecular Sciences, 13, 3038–3072.
Loureiro, J. A., Gomes, B., Coelho, M. A. N., Pereira, M. D., & Rocha, S. (2014). Targeting nanoparticles across the blood-brain barrier with monoclonal antibodies. Nanomedicine, 9, 709–722.
Yang, Z. Z., et al. (2013). Enhanced brain distribution and pharmacodynamics of rivastigmine by liposomes following intranasal administration. International Journal of Pharmaceutics, 452, 344–354.
Salvati, E., et al. (2013). Liposomes functionalized to overcome the blood-brain barrier and to target amyloid-beta peptide: The chemical design affects the permeability across an in vitro model. International Journal of Nanomedicine, 8.
Gobbi, M., et al. (2010). Lipid-based nanoparticles with high binding affinity for amyloid-beta(1–42) peptide. Biomaterials, 31, 6519–6529.
Carrotta, R., Manno, M., Bulone, D., Martorana, V., & San Biagio, P. L. (2005). Protofibril formation of amyloid beta-protein at low pH via a non-cooperative elongation mechanism. Journal of Biological Chemistry, 280, 30001–30008.
Lomakin, A., Chung, D. S., Benedek, G. B., Kirschner, D. A., & Teplow, D. B. (1996). On the nucleation and growth of amyloid beta-protein fibrils: Detection of nuclei and quantitation of rate constants. Proceedings of the National Academy of Sciences of the United States of America, 93, 1125–1129.
Lomakin, A., Teplow, D. B., Kirschner, D. A., & Benedek, G. B. (1997). Kinetic theory of fibrillogenesis of amyloid beta-protein. Proceedings of the National Academy of Sciences of the United States of America, 94, 7942–7947.
Cizas, P., et al. (2010). Size-dependent neurotoxicity of beta-amyloid oligomers. Archives of Biochemistry and Biophysics, 496, 84–92.
Parbhu, A., Lin, H., Thimm, J., & Lal, R. (2002). Imaging real-time aggregation of amyloid beta protein (1–42) by atomic force microscopy. Peptides, 23, 1265–1270.
Streets, A. M., Sourigues, Y., Kopito, R. R., Melki, R., & Quake, S. R. (2013). Simultaneous measurement of amyloid fibril formation by dynamic light scattering and fluorescence reveals complex aggregation kinetics. PloS One, 8.
Blackley, H. K. L., et al. (1999). Morphological development of beta(1–40) amyloid fibrils. Experimental Neurology, 158, 437–443.
Roher, A. E., et al. (2000). Oligomerization and fibril assembly of the amyloid-beta protein. Biochimica Et Biophysica Acta-Molecular Basis of Disease, 1502, 31–43.
Harper, J. D., Wong, S. S., Lieber, C. M., & Lansbury, P. T. (1997). Observation of metastable A beta amyloid protofibrils by atomic force microscopy. Chemistry & Biology, 4, 119–125.
Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., & Teplow, D. B. (1997). Amyloid beta-protein fibrillogenesis—Detection of a protofibrillar intermediate. Journal of Biological Chemistry, 272, 22364–22372.
Harper, J. D., Wong, S. S., Lieber, C. M., & Lansbury, P. T. (1999). Assembly of A beta amyloid protofibrils: An in vitro model for a possible early event in Alzheimer’s disease. Biochemistry, 38, 8972–8980.
Walsh, D. M., et al. (1999). Amyloid beta-protein fibrillogenesis—Structure and biological activity of protofibrillar intermediates. Journal of Biological Chemistry, 274, 25945–25952.
Serem, W. K., Bett, C. K., Ngunjiri, J. N., & Garno, J. C. (2011). Studies of the growth, evolution, and self-aggregation of beta-amyloid fibrils using tapping-mode atomic force microscopy. Microscopy Research and Technique, 74, 699–708.
Gosal, W. S., Clark, A. H., & Ross-Murphy, S. B. (2004). Fibrillar beta-lactoglobulin gels: Part 1. Fibril formation and structure. Biomacromolecules, 5, 2408–2419.
Fändrich, M., Schmidt, M., & Grigorieff, N. (2011). Recent progress in understanding Alzheimer’s β-amyloid structures. Trends in Biochemical Sciences, 36, 338–345.
Schmidt, M., et al. (2009). Comparison of Alzheimer Aβ(1–40) and Aβ(1–42) amyloid fibrils reveals similar protofilament structures. Proceedings of the National Academy of Sciences of the United States of America, 106, 19813–19818.
Arimon, M., et al. (2005). Fine structure study of A beta(1–42) fibrillogenesis with atomic force microscopy. FASEB Journal, 19, 1344.
Moores, B., Drolle, E., Attwood, S. J., Simons, J., & Leonenko, Z. (2011). Effect of surfaces on amyloid fibril formation. PLoS ONE, 6, 8.
Wang, Z. G., et al. (2003). AFM and STM study of beta-amyloid aggregation on graphite. Ultramicroscopy, 97, 73–79.
Fändrich, M., Schmidt, M., & Grigorieff, N. (2011). Recent progress in understanding Alzheimer’s β-amyloid structures. Trends in Biochemical Sciences, 36, 338–345.
Zhang, R., et al. (2009). Interprotofilament interactions between Alzheimer’s A beta(1–42) peptides in amyloid fibrils revealed by cryoEM. Proceedings of the National Academy of Sciences of the United States of America, 106, 4653–4658.
Miyakawa, T., Watanabe, K., & Katsuragi, S. (1986). Ultrastructure of amyloid fibrils in Alzheimers-disease and downs-syndrome. Virchows Archiv B Cell Pathology Including Molecular Pathology, 52, 99–106.
Serpell, L. C. (2000). Alzheimer’s amyloid fibrils: Structure and assembly. Biochimica Et Biophysica Acta-Molecular Basis of Disease, 1502, 16–30.
Serpell, L. C., et al. (1995). Examination of the structure of the transthyretin amyloid fibril by image-reconstruction from electron-micrographs. Journal of Molecular Biology, 254, 113–118.
Miller, Y., Ma, B. Y., Tsai, C. J., & Nussinov, R. (2010). Hollow core of Alzheimer’s A beta(42) amyloid observed by cryoEM is relevant at physiological pH. Proceedings of the National Academy of Sciences of the United States of America, 107, 14128–14133.
Miller, Y., Ma, B. Y., & Nussinov, R. (2011). The unique Alzheimer’s beta-amyloid triangular fibril has a cavity along the fibril axis under physiological conditions. Journal of the American Chemical Society, 133, 2742–2748.
Sachse, C., et al. (2006). Quaternary structure of a mature amyloid fibril from Alzheimer’s A beta(1–40) peptide. Journal of Molecular Biology, 362, 347–354.
Meinhardt, J., Sachse, C., Hortschansky, P., Grigorieff, N., & Fandrich, M. (2009). A beta(1–40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils. Journal of Molecular Biology, 386, 869–877.
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Tinker-Mill, C.L. (2016). Theoretical Concepts of Scanning Probe Microscopy and Dynamic Light Scattering and Their Relation to the Study of Peptide Nanostructures. In: Nanoscale Imaging and Characterisation of Amyloid-β. Springer Theses. Springer, Cham. https://doi.org/10.1007/978-3-319-39534-0_2
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