Engineering amyloidogenicity towards the development of nanofibrillar materials

Trends Biotechnol. 2004 Feb;22(2):93-7. doi: 10.1016/j.tibtech.2003.12.003.

Abstract

When folded into their native structures, proteins in biological systems function as nanostructured machines. By contrast, some polypeptides tend to aggregate into other well-ordered structures, namely amyloid fibrils. Such well-ordered protein fibrils are attractive materials for nanobiotechnology because they self-associate through noncovalent bonds under controlled conditions - a property that is shared with small organic molecules called organogelators. Recently, the use of amyloid fibrils as structural templates for constructing nanowires has been demonstrated. Such applications will potentially become one of the next trends in protein engineering and nanobiotechnology.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amyloid / chemical synthesis
  • Amyloid / chemistry*
  • Biotechnology / instrumentation
  • Biotechnology / methods
  • Contraindications
  • Crystallization / methods*
  • Electronics / instrumentation*
  • Electronics / methods*
  • Macromolecular Substances
  • Nanotechnology / instrumentation*
  • Nanotechnology / methods*
  • Peptides / chemistry*
  • Protein Conformation
  • Protein Engineering / methods*

Substances

  • Amyloid
  • Macromolecular Substances
  • Peptides