Nanostructured peptide fibrils formed at the organic-aqueous interface and their use as templates to prepare inorganic nanostructures

ACS Appl Mater Interfaces. 2009 Apr;1(4):811-5. doi: 10.1021/am800233s.

Abstract

Formation of fibril-type nanostructures of the Alzheimer's beta-amyloid diphenylalanine (l-Phe-l-Phe, FF) at the organic-aqueous interface and the factors affecting their structures have been investigated. Such nanostructures are also formed by bovine serum albumin and bovine pancreas insulin. The concentration of the precursor taken in the aqueous layer plays an important role in determining the morphology of the nanostructures. The addition of curcumin to the organic layer changes the structure of the self-assembled one-dimensional aggregates of diphenylalanine. By coating the diphenylalanine dipeptide fibrils with appropriate precursors followed by calcination in air, it has been possible to obtain one-dimensional nanostructures of inorganic materials.

MeSH terms

  • Crystallization / methods
  • Dipeptides
  • Inorganic Chemicals / chemistry*
  • Materials Testing
  • Nanostructures / chemistry*
  • Nanostructures / ultrastructure
  • Organic Chemicals / chemistry*
  • Particle Size
  • Peptides / chemistry*
  • Phenylalanine / analogs & derivatives*
  • Phenylalanine / chemistry
  • Surface Properties
  • Water / chemistry*

Substances

  • Dipeptides
  • Inorganic Chemicals
  • Organic Chemicals
  • Peptides
  • Water
  • phenylalanylphenylalanine
  • Phenylalanine