Self-assembled peptide fibers from valylvaline bola-amphiphiles by a parallel beta-sheet network

Biochim Biophys Acta. 2000 Jul 26;1475(3):346-52. doi: 10.1016/s0304-4165(00)00088-x.

Abstract

A series of dipeptide-based bola-amphiphiles, bis(N-alpha-amide-L-valyl-L-valine) 1, n-alkane dicarboxylate (n=4-12), have been synthesized. The bola-amphiphiles with n=4 and 6 self-assembled to form crystalline solids in water, whereas those with n=7-12 produced peptide fibers. FT-IR spectroscopy and X-ray diffraction patterns revealed that the peptide fibers have parallel-type beta-sheet networks between the valylvaline units. FT-IR deconvolution study of carboxyl regions indicated that these crystalline solids and peptide fibers are stabilized by interlayer bifurcated and intralayer lateral hydrogen-bond networks between the end carboxylic acid groups, respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Hydrogels
  • Hydrogen Bonding
  • Microscopy, Electron / methods
  • Models, Molecular
  • Molecular Weight
  • Particle Size
  • Peptides / chemical synthesis*
  • Protein Structure, Secondary*
  • Spectroscopy, Fourier Transform Infrared
  • Surface-Active Agents / chemistry*
  • X-Ray Diffraction

Substances

  • Hydrogels
  • Peptides
  • Surface-Active Agents