Modulating materials by orthogonally oriented β-strands: composites of amyloid and silk fibroin fibrils

Adv Mater. 2014 Jul 9;26(26):4569-74. doi: 10.1002/adma.201400730. Epub 2014 May 20.

Abstract

Amyloid fibrils and silk fibroin (SF) fibrils are proteinaceous aggregates occurring either naturally or as artificially reconstituted fibrous systems, in which the constituent β-strands are aligned either orthogonally or parallel to the fibril main axis, conferring complementary physical properties. Here, it is shown how the combination of these two classes of protein fibrils with orthogonally oriented β-strands results in composite materials with controllable physical properties at the molecular, mesoscopic, and continuum length scales.

Keywords: amyloid fibrils; molecular orientation; nanocomposites; silk fibroin; β-strands; β-sheets.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid / chemistry*
  • Amyloid / ultrastructure
  • Animals
  • Biocompatible Materials / chemistry
  • Biomechanical Phenomena
  • Fibroins / chemistry*
  • Fibroins / ultrastructure
  • Lactoglobulins / chemistry
  • Lactoglobulins / ultrastructure
  • Materials Testing
  • Microscopy, Atomic Force
  • Microscopy, Electron, Scanning
  • Models, Molecular
  • Protein Structure, Secondary
  • Tensile Strength
  • X-Ray Diffraction

Substances

  • Amyloid
  • Biocompatible Materials
  • Lactoglobulins
  • Fibroins