Nanomaterials: amyloids reflect their brighter side

Article English OPEN
Maji, Samir Kumar ; Mankar, Shruti ; Anoop, A. ; Sen, Shamik (2011)
  • Publisher: Co-Action Publishing
  • Journal: Nano Reviews, volume 2 (eissn: 2000-5121)
  • Related identifiers: pmc: PMC3215191, doi: 10.3402/nano.v2i0.6032, doi: 10.3402/nr.v2i0.6032
  • Subject: self-assembly | stem cells | Review Article | tissue engineering | nanowires | Nanotechnology; self-assembly; peptide/protein; fibrils; tissue engineering; stem cells; drug delivery; nanowires | Nanotechnology | drug delivery | peptide/protein | fibrils
    mesheuropmc: mental disorders

Amyloid fibrils belong to the group of ordered nanostructures that are self-assembled from a wide range of polypeptides/ proteins. Amyloids are highly rigid structures possessing a high mechanical strength. Although amyloids have been implicated in the pathogenesis of several human diseases, growing evidence indicates that amyloids may also perform native functions in host organisms. Discovery of such amyloids, referred to as functional amyloids, highlight their possible use in designing novel nanostructure materials. This review summarizes recent advances in the application of amyloids for the development of nanomaterials and prospective applications of such materials in nanotechnology and biomedicine. Keywords: Nanotechnology; self-assembly; peptide/protein; fibrils; tissue engineering; stem cells; drug delivery; nanowires (Published: 31 May 2011) Citation: Nano Reviews 2011, 2: 6032 - DOI: 10.3402/nano.v2i0.6032
  • References (102)
    102 references, page 1 of 11

    1. Alberts B, Bray D, Lewis J, Raff M, Roberts K, Watson JD. Molecular biology of the cell. New York: Garland Science; 2002.

    2. Smith JF, Knowles TP, Dobson CM, Macphee CE, Welland ME. Characterization of the nanoscale properties of individual amyloid fibrils. Proc Natl Acad Sci USA 2006; 103: 15806 11.

    3. Knowles TP, Fitzpatrick AW, Meehan S, Mott HR, Vendruscolo M, Dobson CM, et al. Role of intermolecular forces in defining material properties of protein nanofibrils. Science 2007; 318: 1900 3.

    4. Gazit E. Self-assembled peptide nanostructures: the design of molecular building blocks and their technological utilization. Chem Soc Rev 2007; 36: 1263 9.

    5. Zhang S. Fabrication of novel biomaterials through molecular self-assembly. Nat Biotechnol 2003; 21: 1171 8.

    6. Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 2006; 75: 333 66.

    7. Cherny I, Gazit E. Amyloids: not only pathological agents but also ordered nanomaterials. Angew Chem Int Ed Engl 2008; 47: 4062 9.

    8. Gras SL, Tickler AK, Squires AM, Devlin GL, Horton MA, Dobson CM, et al. Functionalised amyloid fibrils for roles in cell adhesion. Biomaterials 2008; 29: 1553 62.

    9. Gras SL. Surface- and Solution-Based Assembly of Amyloid Fibrils for Biomedical and Nanotechnology Applications. Adv Chem Eng 2009; 35: 161 209.

    10. Maji SK, Wang L, Greenwald J, Riek R. Structure-activity relationship of amyloid fibrils. FEBS Lett 2009; 583: 2610 7.

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