Alpha-helix stabilization within a peptide dendrimer

J Am Chem Soc. 2008 Dec 24;130(51):17248-9. doi: 10.1021/ja8076236.


The alpha-helical second generation peptide dendrimer of sequence (AcAMEA)(4)(KKLME)(2)KMKLA is more stable than the corresponding linear peptide AcAMEAAKLMEAMKLA toward pH-induced unfolding and temperature-induced intermolecular aggregation. The effect is interpreted in terms of an alpha-helix spanning across two successive branching points of the dendrimer. This stabilization effect is unprecedented and opens the way to folded dendritic analogues of proteins using natural amino acids only.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / chemistry
  • Chemistry / methods*
  • Circular Dichroism / methods
  • Dendrimers
  • Hydrogen-Ion Concentration
  • Models, Molecular
  • Molecular Conformation
  • Peptides / chemistry
  • Protein Conformation
  • Protein Structure, Secondary
  • Proteins / chemistry
  • Spectroscopy, Fourier Transform Infrared
  • Temperature


  • Amino Acids
  • Dendrimers
  • Peptides
  • Proteins