Aqueous self-assembly of unsymmetric Peptide bolaamphiphiles into nanofibers with hydrophilic cores and surfaces

J Am Chem Soc. 2003 Oct 22;125(42):12680-1. doi: 10.1021/ja035882r.

Abstract

Unsymmetric peptide bolaamphiphiles that incorporate (l-glutamyl)3glycine at one terminus and either tetraethylene glycol or aspartic acid at the other were found to form hydrogels at low wt %, presumably by self-assembling into nanofibers presenting (l-glutamyl)3glycine at their surfaces and burying the second headgroup at their cores. Transmission electron microscopy measurements on 1 wt % gels negatively stained with phosphotungstic acid and positively stained with uranyl acetate show one-dimensional objects with diameters of 5 nm and lengths in excess of 1 mum. Circular dichroism and solid-state FTIR spectra indicate the adoption of beta-sheet structure within the nanofibers.

Publication types

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

MeSH terms

  • Alanine / analogs & derivatives
  • Circular Dichroism
  • Glycine / analogs & derivatives
  • Hydrophobic and Hydrophilic Interactions
  • Models, Molecular
  • Nanotubes, Peptide / chemistry*
  • Peptides / chemistry*
  • Protein Structure, Secondary
  • Spectroscopy, Fourier Transform Infrared
  • Surface Properties
  • Water / chemistry*

Substances

  • Nanotubes, Peptide
  • Peptides
  • Water
  • Alanine
  • Glycine