Bilayer fibril formation by genetically engineered polypeptides: preparation and characterization

Biomacromolecules. 2006 Apr;7(4):1104-11. doi: 10.1021/bm0509016.

Abstract

A de novo, genetically engineered 687 residue polypeptide expressed in E. coli has been found to form highly rectilinear, beta-sheet containing fibrillar structures. Tapping-mode atomic force microscopy, deep-UV Raman spectroscopy, and transmission electron microscopy definitively established the tendency of the fibrils to predominantly display an apparently planar bilayer or ribbon assemblage. The ordered self-assembly of designed, extremely repetitive, high molecular weight peptides is a harbinger of the utility of similar materials in nanoscience and engineering applications.

Publication types

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

MeSH terms

  • Base Sequence
  • DNA / chemistry
  • DNA / genetics
  • Lipid Bilayers / chemical synthesis*
  • Lipid Bilayers / chemistry*
  • Lipid Bilayers / isolation & purification
  • Microscopy, Atomic Force
  • Microscopy, Electron, Transmission
  • Molecular Sequence Data
  • Molecular Weight
  • Particle Size
  • Peptides / chemical synthesis*
  • Peptides / chemistry*
  • Peptides / isolation & purification
  • Protein Conformation
  • Protein Engineering*
  • Protein Structure, Secondary
  • Sensitivity and Specificity
  • Spectrum Analysis, Raman

Substances

  • Lipid Bilayers
  • Peptides
  • DNA