Design and Construction of Large Amyloid Fibers

Article, Other literature type English OPEN
Ridgley, Devin M.; Rippner, Caitlin M. W.; Barone, Justin R.;
(2015)
  • Publisher: MDPI AG
  • Journal: Fibers (issn: 2079-6439)
  • Publisher copyright policies & self-archiving
  • Identifiers: doi: 10.3390/fib3020090
  • Subject: TP200-248 | fiber | Textile bleaching, dyeing, printing, etc. | QH301-705.5 | β-sheet | amyloid | protein | Physics | QC1-999 | Chemicals: Manufacture, use, etc. | Biology (General) | TP890-933
    mesheuropmc: musculoskeletal system | technology, industry, and agriculture

Mixtures of “template” and “adder” proteins self-assemble into large amyloid fibers of varying morphology and modulus. Fibers range from low modulus, rectangular cross-sectioned tapes to high modulus, circular cross-sectioned cylinders. Varying the proteins in the mixtu... View more
  • References (41)
    41 references, page 1 of 5

    1. Knowles, T.P.J.; Buehler, M.J. Nanomechanics of functional and pathological amyloid materials. Nat. Nanotechnol. 2011, 6, 469-479.

    2. Fowler, D.M.; Koulov, A.V.; Balch, W.E.; Kelly, J.W. Functional amyloid-from bacteria to humans. Trends Biochem. Sci. 2007, 32, 217-224.

    3. Adamcik, J.; Jung, J.-M.; Flakowski, J.; de Los Rios, P.; Dietler, G.; Mezzenga, R. Understanding amyloid aggregation by statistical analysis of atomic force microscopy images. Nat. Nanotechnol. 2010, 5, 423-428.

    4. Bolisetty, S.; Adamcik, J.; Mezzenga, R. Snapshots of fibrillation and aggregation kinetics in multistranded amyloid β-lactoglobulin fibrils. Soft Matter 2011, 7, 493-499.

    5. Aggeli, A.; Nyrkova, I.A.; Bell, M.; Harding, R.; Carrick, L.; McLeish, T.C.B.; Semenov, A.N.; Boden, N. Hierarchical self-assembly of chiral rod-like molecules as a model for peptide β-sheet tapes, ribbons, fibrils, and fibers. Proc. Natl. Acad. Sci. USA 2001, 98, 11857-11862.

    6. Barlow, D.E.; Dickinson, G.H.; Orihuela, B.; Kulp III, J.L.; Rittschof, D.; Wahl, K.J. Characterization of the adhesive plaque of the barnacle Balanus amphitrite: Amyloid-like nanofibrils are a major component. Langmuir 2010, 26, 6549-6556.

    7. Gebbink, M.F.B.G.; Claessen, D.; Bouma, B.; Dijkhuizen, L.; Wosten, H.A.B. Amyloids-A functional coat for microorganisms. Nat. Rev. Microbiol. 2005, 3, 333-341.

    8. Hammer, N.D.; Schmidt, J.C.; Chapman, M.R. The curli nucleator protein, csgb, contains an amyloidogenic domain that directs csga polymerization. Proc. Natl. Acad. Sci. USA 2007, 104, 12494-12499.

    9. Alsteens, D.; Ramsook, C.B.; Lipke, P.N.; Dufrêne, Y.F. Unzipping a functional microbial amyloid. ACS Nano 2012, 6, 7703-7711.

    10. Parker, K.D.; Rudall, K.M. Structure of the silk of Chrysopa egg-stalks. Nature 1957, 179, 905-906.

  • Related Research Results (1)
    Inferred by OpenAIRE
    dataset
    Overview of Approach and Techniques Used (2015)
    65%
  • Related Organizations (2)
  • Metrics
Share - Bookmark