Alpha-helix stabilization within a peptide dendrimer.
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.
Javor
Sacha
S
Department of Chemistry and Biochemistry, University of Berne, Freiestrasse 3, CH-3012 Berne, Switzerland.
Natalello
Antonino
A
Doglia
Silvia Maria
SM
Reymond
Jean-Louis
JL
D000596:Amino Acids / Q000737:chemistry; D002621:Chemistry / Q000379:methods*; D002942:Circular Dichroism / Q000379:methods; D050091:Dendrimers; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature
D000596:Amino Acids; D050091:Dendrimers; D010455:Peptides; D011506:Proteins