Nanostructured films from hierarchical self-assembly of amyloidogenic proteins

Nature Nanotechnology

Volumn 5, Issue 3, 2010, Pages 204-207

  Knowles, Tuomas P J ^a   Oppenheim, Tomas W ^a   Buell, Alexander K ^a   Chirgadze, Dimitri Y ^a   Welland, Mark E ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ELASTIC MODULI; FUNCTIONAL MATERIALS; NANOSTRUCTURED MATERIALS; NANOTECHNOLOGY; PROTEINS; SCAFFOLDS (BIOLOGY); SELF ASSEMBLY; FILMS;

AMYLOIDOGENIC PROTEINS; BIOMOLECULAR INTERACTIONS; CONTROLLED ASSEMBLY; HIERARCHICAL SELF-ASSEMBLY; MACROSCOPIC MATERIALS; MULTI-FUNCTIONAL MATERIALS; NANOSTRUCTURED FILMS; PROTEINACEOUS MATERIALS; FREESTANDING FILMS; PROTEIN SCAFFOLDS;

FILMS; PROTEINS;

AMYLOID PROTEIN; FLUORESCENT DYE; FLUOROPHORE; NANOFILM; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; FIBER; FILM; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN STRUCTURE; YOUNG MODULUS;

EID: 77949261467     PISSN: 17483387     EISSN: 17483395     Source Type: Journal    
DOI: 10.1038/nnano.2010.26     Document Type: Article

References (30)

1. Dobson, C. M. Protein folding and misfolding. Nature 426, 884-890 (2003).
2. Buehler, M. J. & Ackbarow, T. Nanomechanical strength mechanisms of hierarchical biological materials and tissues. Comput. Methods Biomech. Biomed. Eng. 11, 595-607 (2008).
3. Buehler, M. J. & Yung, Y. C. Deformation and failure of protein materials in physiologically extreme conditions and disease. Nature Mater. 8, 175-188 (2009).
4. Whitesides, G. M. & Grzybowski, B. Self-assembly at all scales. Science 295, 2418-2421 (2002).
5. Kol, N. et al. Self-assembled peptide nanotubes are uniquely rigid bioinspired supramolecular structures. Nano Lett. 5, 1343-1346 (2005).
6. Zhang, S. Fabrication of novel biomaterials through molecular self-assembly. Nature Biotechnol. 21, 1171-1178 (2003).
7. Mao, C. et al. Virus-based toolkit for the directed synthesis of magnetic and semiconducting nanowires. Science 303, 213-217 (2004).
8. Rothemund, P. W. K. Folding DNA to create nanoscale shapes and patterns. Nature 440, 297-302 (2006).
9. Zhang, S., Holmes, T., Lockshin, C. & Rich, A. Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane. Proc. Natl Acad. Sci. USA 90, 3334-3338 (1993).
10. Goodman, R. P. et al. Rapid chiral assembly of rigid DNA building blocks for molecular nanofabrication. Science 310, 1661-1665 (2005).
11. Chiti, F. & Dobson, C. M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366 (2006).
12. Kelly, J.W. Towards an understanding of amyloidogenesis. Nature Struct. Biol. 9, 323-325 (2002).
13. Dobson, C. M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24, 329-332 (1999).
14. Fändrich, M., Fletcher, M. A. & Dobson, C. M. Amyloid fibrils from myoglobin. Nature 410, 165-166 (2001).
15. Fowler, D. M., Koulov, A. V., Balch, W. E. & Kelly, J. W. Functional amyloid - from bacteria to humans. Trends Biochem. Sci. 32, 217-224 (2007).
16. Chapman, M. R. et al. Role of Escherichia coli curli operons in directing amyloid fiber formation. Science 295, 851-855 (2002).
17. Maji, S. K. et al. Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325, 328-332 (2009).
18. Huang, Y., Duan, X., Wei, Q. & Lieber, C.M. Directed assembly of one-dimensional nanostructures into functional networks. Science 291, 630-633 (2001).
19. Ikkala, O. & ten Brinke, G. Functional materials based on self-assembly of polymeric supramolecules. Science 295, 2407-2409 (2002).
20. Knowles, T. P. et al. Role of intermolecular forces in defining material properties of protein nanofibrils. Science 318, 1900-1903 (2007).
21. Reches, M. & Gazit, E. Controlled patterning of aligned self-assembled peptide nanotubes. Nature Nanotech. 1, 195-200 (2006).
22. Gennadios, A. (ed.) Protein Based Films and Coatings (CRC Press, 2002).
23. Sawaya, M. R. et al. Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature 447, 453-457 (2007).
24. Jaroniec, C. P. et al. High resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy. Proc. Natl Acad. Sci. USA 101, 711-716 (2004).
25. Donald, A. M.,Windle, A. H. & Hanna, S. Liquid Crystalline Polymers 2nd edn (Cambridge Univ. Press, 2006).
26. Corrigan, A. M., Müller, C. & Krebs, M. R. H. The formation of nematic liquid crystal phases by hen lysozyme amyloid fibrils. J. Am. Chem. Soc. 129, 14740-14741 (2006).
27. Smith, J. F., Knowles, T. P. J., Dobson, C. M., Macphee, C. E. & Welland, M. E. Characterization of the nanoscale properties of individual amyloid fibrils. Proc. Natl Acad. Sci. USA 103, 15806-15811 (2006).
28. Baughman, R. H., Zakhidov, A. A. & de Heer, W. A. Carbon nanotubes - the route toward applications. Science 297, 787-792 (2002).
29. Krebs, M. R. H., Bromley, E. H. C. & Donald, A. M. The binding of thioflavin-T to amyloid fibrils: localisation and implications. J. Struct. Biol. 149, 30-37 (2005).
30. Kosevich, A. M., Lifshitz, E. M., Landau, L. D. & Pitaevskii, L. P. Theory of Elasticity (Butterworth-Heinemann, 1986).