Time-lapse atomic force microscopy in the characterization of amyloid-like fibril assembly and oligomeric intermediates

Methods in Molecular Biology

Volumn 299, Issue , 2005, Pages 103-128

  Goldsbury, Claire ^a   Green, Janelle ^b  

^a MAX PLANCK UNIT FOR STRUCTURAL MOLECULAR BIOLOGY   (Germany)

^b UNIVERSITY OF BASEL   (Switzerland)

Author keywords

Alzheimer s disease; Amylin; Amyloid fibril; Amyloid protein (A ); Fibril assembly; Fibril structure; Islet amyloid polypeptide (IAPP); Oligomeric intermediates; Protofibril; Time lapse atomic force microscopy

Indexed keywords

AMYLOID PROTEIN; OLIGOMER;

AMINO ACID SEQUENCE; ATOMIC FORCE MICROSCOPY; DECONTAMINATION; ELECTRON MICROSCOPY; HUMAN; LIPID BILAYER; PH; PROTEIN ASSEMBLY; PROTEIN IMMOBILIZATION; SURFACE PROPERTY; TIME-LAPSE MICROSCOPY;

EID: 22844448175     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1385/1-59259-874-9:103     Document Type: Chapter

References (37)

1. Goldsbury, C., Kistler, J., Aebi, U., Arvinte, T., and Cooper, G. J. S. (1999) Watching amyloid fibrils grow by time-lapse atomic force microscopy. J. Mol. Biol. 285, 33-39.
2. Green, J., Goldsbury, C., Mini, T., et al. (2003) Full-length rat amylin forms fibrils following substitution of single residues from human amylin. J. Mol. Biol. 326, 1147-1156.
3. Green, J. D., Goldsbury, C., Kistler, J., Cooper, G. J. S., and Aebi, U. (2004) Human amylin oligomer growth and fibril elongation define two distinct phases in amyloid formation. J. Biol. Chem. 279, 12206-12212.
4. Allison, D. P., Hinterdorfer, P., and Han, W. (2002) Biomolecular force measurements and the atomic force microscope. Curr. Opin. Biotechnol. 13, 47-51.
5. Engel, A. and Muller, D. J. (2000) Observing single biomolecules at work with the atomic force microscope. Nat. Struct. Biol. 7, 715-718.
6. Fisher, T. E., Marszalek, P. E., and Fernandez, J. M. (2000) Stretching single molecules into novel conformations using the atomic force microscope. Nat. Struct. Biol. 7, 719-724.
7. Stolz, M., Stoffler, D., Aebi, U., and Goldsbury, C. (2000) Monitoring biomolecular interactions by time-lapse atomic force microscopy. J. Struct. Biol. 131, 171-180.
8. Engel, A., Lyubchenko, Y., and Muller, D. (1999) Atomic force microscopy: a powerful tool to observe biomolecules at work. Trends Cell Biol. 9, 77-80.
9. Engel, A., Gaub, H. E., and Muller, D. J. (1999) Atomic force microscopy: a forceful way with single molecules. Curr. Biol. 9, R133-R136.
10. Heinz, W. F. and Hoh, J. H. (1999) Spatially resolved force spectroscopy of biological surfaces using the atomic force microscope. Trends Biotechnol. 17, 143-150.
11. Hansma, H. G., Kim, K. J., Laney, D. E., et al. (1997) Properties of biomolecules measured from atomic force microscope images: a review. J. Struct. Biol. 119, 99-108.
12. Bustamante, C., Rivetti, C., and Keller, D. J. (1997) Scanning force microscopy under aqueous solutions. Curr. Opin. Struct. Biol. 7, 709-716.
13. Lal, R. and John, S. A. (1994) Biological applications of atomic force microscopy. Am. J. Physiol. 266, C1-C21.
14. Clausen-Schaumann H., Seitz, M., Krautbauer, R., and Gaub, H. E. (2000) Force spectroscopy with single bio-molecules. Curr. Opin. Chem. Biol. 4(5), 524-530.
15. Goldsbury, C., Aebi, U., and Frey, P. (2001) Visualizing the growth of Alzheimer’s Aβ?amyloid-like fibrils. Trends Mol. Med. 7, 582.
16. Czajkowsky, D. M. and Shao, Z. (2002) Supported lipid bilayers as effective substrates for atomic force microscopy. Methods Cell Biol. 68, 231-241.
17. Rinia, H. A., Kik, R. A., Demel, R. A., et al. (2000) Visualization of highly ordered striated domains induced by transmembrane peptides in supported phosphatidylcholine bilayers. Biochemistry 39, 5852-5858.
18. Shi, D., Somlyo, A. V., Somlyo, A. P., and Shao, Z. (2001) Visualizing filamentous actin on lipid bilayers by atomic force microscopy in solution. J. Microsc. 201(Pt 3), 377-382.
19. Goldsbury, C. S., Cooper, G. J., Goldie, K. N., et al. (1997) Polymorphic fibrillar assembly of human amylin. J. Struct. Biol. 119, 17-27.
20. Kammerer, R. A., Kostrewa, D., Zurdo, J., et al. (2004) Exploring amyloid formation by a de novo design. Proc. Natl. Acad. Sci. USA 101, 4435-4440.
21. Sharp, J. S., Forrest, J. A., and Jones, R. A. (2002) Surface denaturation and amyloid fibril formation of insulin at model lipid-water interfaces. Biochemistry 41, 15810-15819.
22. Aitken, J. F., Loomes, K. M., Konarkowska, B., and Cooper, G. J. S. (2003) Suppression by polycyclic compounds of the conversion of human amylin into insoluble amyloid. Biochem. J. 374, 779-784.
23. Goldsbury, C. S., Wirtz, S., Müller, S. A., et al. (2000) Studies on the in vitro assembly of Aβ1-40: implications for the search for Aβ?fibril formation inhibitors. J. Struct. Biol. 130, 217-231.
24. Green, J. D., Kreplak, L., Goldsbury, C. et al. (2004) Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptides. J. Mol. Biol., in press.
25. Janson, J., Ashley, R. H., Harrison, D., McIntyre, S., and Butler, P. C. (1999) The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. Diabetes 48, 491-498.
26. Kagan, B. L., Hirakura, Y., Azimov, R., Azimova, R., and Lin, M. C. (2002) The channel hypothesis of Alzheimer’s disease: current status. Peptides 23, 1311-1315.
27. Anguiano, M., Nowak, R. J., and Lansbury, P. T. Jr. (2002) Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes. Biochemistry 41, 11338-11343.
28. Harroun, T. A., Bradshaw, J. P., and Ashley, R. H. (2001) Inhibitors can arrest the membrane activity of human islet amyloid polypeptide independently of amyloid formation. FEBS Lett. 507, 200-204.
29. Padrick, S. B. and Miranker, A. D. (2002) Islet amyloid: phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis. Biochemistry 41, 4694-4703.
30. Schabert, F. A. and Engel, A. (1994) Reproducible acquisition of Escherichia coli porin surface topographs by atomic force microscopy. Biophys. J. 67, 2394-2403.
31. Karrasch, S., Dolder, M., Schabert, F., Ramsden, J., and Engel, A. (1993) Covalent binding of biological samples to solid supports for scanning probe microscopy in buffer solution. Biophys. J. 65, 2437-2446.
32. Reviakine, I. and Brisson, A. (2000) Formation of supported phospholipid bilayers from unilamellar vesicles investigated by atomic force microscopy. Langmuir 16, 1806-1815.
33. Allen, M. J., Hud, N. V., Balooch, M., Tench, R. J., Siekhaus, W. J., and Balhorn, R. (1992) Tip-radius-induced artifacts in AFM images of protamine-complexed DNA fibers. Ultramicroscopy 42-44(Pt B), 1095-1100.
34. Willemsen, O. H., Snel, M. M., van der Werf, K. O., et al. (1998) Simultaneous height and adhesion imaging of antibody-antigen interactions by atomic force microscopy. Biophys. J. 75(5), 2220-2228.
35. Xu, S., Bevis, B., and Arnsdorf, M. F. (2001) The assembly of amyloidogenic yeast sup35 as assessed by scanning (atomic) force microscopy: an analogy to linear colloidal aggregation? Biophys. J. 81, 446-454.
36. Markiewicz, P. (1988) Orientational Dependency of Atomic Force Microscopic Images Revealed by Alzheimer Paired Helical Filaments. In: Doctoral Thesis, Department of Chemistry, University of Toronto.
37. Muller, D. J. and Engel, A. (1997) The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions. Biophys. J. 73, 1633-1644.